eF-site ID 4kn7-ABCDEFGHIJXY PDB Code 4kn7 Chain A, B, C, D, E, F, G, H, I, J, X, Y Title X-ray crystal structure of the Escherichia coli RNA polymerase in complex with Benzoxazinorifamycin-2c Classification TRANSFERASE/ANTIBIOTIC Compound DNA-directed RNA polymerase subunit alpha Source Escherichia coli (strain K12) (RPOD_ECOLI) Sequence A:  GSVTEFLKPRLVDIEQVSSTHAKVTLEPLERGFGHTLGNA LRRILLSSMPGCAVTEVEIDGVLHEYSTKEGVQEDILEIL LNLKGLAVRVQGKDEVILTLNKSGIGPVTAADITHDGDVE IVKPQHVICHLTDENASISMRIKVQRGRGYVPASTRIHSE EDERPIGRLLVDACYSPVERIAYNVEAARVEQRTDLDKLV IEMETNGTIDPEEAIRRAATILAEQLEAFVDLRDVRQPEV KEEKPEFDPILLRPVDDLELTVRSANCLKAEAIHYIGDLV QRTEVELLKTPNLGKKSLTEIKDVLASRGLSLGMRLENWP PAS B:  TEFLKPRLVDIEQVSSTHAKVTLEPLERGFGHTLGNALRR ILLSSMPGCAVTEVEIDGVLHEYSTKEGVQEDILEILLNL KGLAVRVQGKDEVILTLNKSGIGPVTAADITHDGDVEIVK PQHVICHLTDENASISMRIKVQRGRGYVPASTIGRLLVDA CYSPVERIAYNVEAARVEQRTDLDKLVIEMETNGTIDPEE AIRRAATILAEQLEAFVDLRD C:  KKRIRKDFGKRPQVLDVPYLLSIQLDSFQKFIEQDPEGQY GLEAAFRSVFPIQSYSGNSELQYVSYRLGEPVFDVQECQI RGVTYSAPLRVKLRLVIYEREAPEGTVKDIKEQEVYMGEI PLMTDNGTFVINGTERVIVSQLHRSPGVFFDSDKGKTHSS GKVLYNARIIPYRGSWLDFEFDPKDNLFVRIDRRRKLPAT IILRALNYTTEQILDLFFEKVIFEIRDNKLQMELVPERLR GETASFDIEANGKVYVEKGRRITARHIRQLEKDDVKLIEV PVEYIAGKVVAKDYIDESTGELICAANMELSLDLLAKLSQ SGHKRIETLFTNDLDHGPYISETLRVDPTNDRLSALVEIY RMMRPGEPPTREAAESLFENLFFSEDRYDLSAVGRMKFNR SLLREEIEGSGILSKDDIIDVMKKLIDIRNGKGEVDDIDH LGNRRIRSVGEMAENQFRVGLVRVERAVKERLSLGDLDTL MPQDMINAKPISAAVKEFFGSSQLSQFMDQNNPLSEITHK RRISALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGP NIGLINSLSVYAQTNEYGFLETPYRKVTDGVVTDEIHYLS AIEEGNYVIAQANSNLDEEGHFVEDLVTCRSKGESSLFSR DQVDYMDVSTQQVVSVGASLIPFLEHDDANRALMGANMQR QAVPTLRADKPLVGTGMERAVAVDSGVTAVAKRGGVVQYV DASRIVIKVNEDEMYPGEAGIDIYNLTKYTRSNQNTCINQ MPCVSLGEPVERGDVLADGPSTDLGELALGQNMRVAFMPW NGYNFEDSILVSERVVQEDRFTTIHIQELACVSRDTKLGP EEITADIPNVGEAALSKLDESGIVYIGAEVTGGDILVGKV TPKGETQLTPEEKLLRAIFGEKASDVKDSSLRVPNGVSGT VIDVQVFTRDGVEKDKRALEIEEMQLKQAKKDLSEELQIL EAGLFSRIRAVLVAGGVEAEKLDKLPRDRWLELGLTDEEK QNQLEQLAEQYDELKHEFEKKLEAKRRKITQGDDLAPGVL KIVKVYLAVKRRIQPGDKMAGRHGNKGVISKINPIEDMPY DENGTPVDIVLNPLGVPSRMNIGQILETHLGMAAKGIGDK INAMLKQQQEVAKLREFIQRAYDLGADVRQKVDLSTFSDE EVMRLAENLRKGMPIATPVFDGAKEAEIKELLKLGDLPTS GQIRLYDGRTGEQFERPVTVGYMYMLKLNHLVDDKMHARS TGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTL QEMLTVKSDDVNGRTKMYKNIVDGNHQMEPGMPESFNVLL KEIRSLGINIELEDE D:  LKAQTKTEEFDAIKIALASPDMIRSWSFGEVKKPETINYR TFKPERDGLFCARIFGPVKDYECLCGKYKRLKHRGVICEK CGVEVTQTKVRRERMGHIELASPTAHIWFLKSLPSRIGLL LDMPLRDIERVLYFESYVVIEGGMTNLERQQILTEEQYLD ALEEFGDEFDAKMGAEAIQALLKSMDLEQECEQLREELNE TNSETKRKKLTKRIKLLEAFVQSGNKPEWMILTVLPVLPP DLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLLDLAA PDIIVRNEKRMLQEAVDALLDNGRRGRAITGSNKRPLKSL ADMIKGGKRVDYSGRSVITVGPYLRLHQCGLPKKMALELF KPFIYGKLELRGLATTIKAAKKMVEREEAVVWDILDEVIR EHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCAAY NADFDGDQMAVHVPLTLEAQLEARALMMSTNNILSPANGE PIIVPSQDVVLGLYYMTRDCVNAKGEGMVLTGPKEAERLY RSGLASLHARVKVRITEYEKDANGELVAKTSLKDTTVGRA ILWMIVPKGLPYSIVNQALGKKAISKMLNTCYRILGLKPT VIFADQIMYTGFAYAARSGASVGIDDMVIPEKKHEIISEA EAEVAEIQEQFQSGLVTAGERYNKVIDIWAAANDRVSKAM MDNLQTETVINRDGQEEKQVSFNSIYMMADSGARGSAAQI RQLAGMRGLMAKPDGSIIETPITANFREGLNVLQYFISTH GARKGLADTALKTANSGYLTRRLVDVAQDLVVTEDDCGTH EGIMMTPVIEGGDVKEPLRDRVLGRVTAEDVLKPGTADIL VPRNTLLHEQWCDLLEENSVDAVKVRSVVSCDTDFGVCAH CYGRDLARGHIINKGEAIGVIAAQSIGEPGTQLTMRDITG GLPRVADLFEARRPKEPAILAEISGIVSFGKETKGKRRLV ITPVDGSDPYEEMIPKWRQLNVFEGERVERGDVISDGPEA PHDILRLRGVHAVTRYIVNEVQDVYRLQGVKINDKHIEVI VRQMLRKATIVNAGSSDFLEGEQVEYSRVKIANRELEANG KVGATYSRDLLGITKASLATESFISAASFQETTRVLTEAA VAGKRDELRGLKENVIVGRLIPAGTGYAYHQDRMRRRAAG E:  ARVTVQDAVEKIGNRFDLVLVAARRARQMQVGGKDPLVPE ENDKTTVIALREIEEGLINNQILDVRERQEQQEQEAAELQ AVTAIAEGRR F:  TEFLKPRLVDIEQVSSTHAKVTLEPLERGFGHTLGNALRR ILLSSMPGCAVTEVEIDGVLHEYSTKEGVQEDILEILLNL KGLAVRVQGKDEVILTLNKSGIGPVTAADITHDGDVEIVK PQHVICHLTDENASISMRIKVQRGRGYVPASTRIHSEEDE RPIGRLLVDACYSPVERIAYNVEAARVEQRTDLDKLVIEM ETNGTIDPEEAIRRAATILAEQLEAFVDL G:  TEFLKPRLVDIEQVSSTHAKVTLEPLERGFGHTLGNALRR ILLSSMPGCAVTEVEIDGVLHEYSTKEGVQEDILEILLNL KGLAVRVQGKDEVILTLNKSGIGPVTAADITHDGDVEIVK PQHVICHLTDENASISMRIKVQRGRGYVPASTIGRLLVDA CYSPVERIAYNVEAARVEQRTDLDKLVIEMETNGTIDPEE AIRRAATILAEQLEAFV H:  KKRIRKDFGKRPQVLDVPYLLSIQLDSFQKFIEQDPEGQY GLEAAFRSVFPIQSYSGNSELQYVSYRLGEPVFDVQECQI RGVTYSAPLRVKLRLVIYEREAPEGTVKDIKEQEVYMGEI PLMTDNGTFVINGTERVIVSQLHRSPGVFFDSDKGKTHSS GKVLYNARIIPYRGSWLDFEFDPKDNLFVRIDRRRKLPAT IILRALNYTTEQILDLFFEKVIFEIRDNKLQMELVPERLR GETASFDIEANGKVYVEKGRRITARHIRQLEKDDVKLIEV PVEYIAGKVVAKDYIDESTGELICAANMELSLDLLAKLSQ SGHKRIETLFTNDLDHGPYISETLRVDPTNDRLSALVEIY RMMRPGEPPTREAAESLFENLFFSEDRYDLSAVGRMKFNR SLLREEIEGSGILSKDDIIDVMKKLIDIRNGKGEVDDIDH LGNRRIRSVGEMAENQFRVGLVRVERAVKERLSLGDLDTL MPQDMINAKPISAAVKEFFGSSQLSQFMDQNNPLSEITHK RRISALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGP NIGLINSLSVYAQTNEYGFLETPYRKVTDGVVTDEIHYLS AIEEGNYVIAQANSNLDEEGHFVEDLVTCRSKGESSLFSR DQVDYMDVSTQQVVSVGASLIPFLEHDDANRALMGANMQR QAVPTLRADKPLVGTGMERAVAVDSGVTAVAKRGGVVQYV DASRIVIKVNEDEMYPGEAGIDIYNLTKYTRSNQNTCINQ MPCVSLGEPVERGDVLADGPSTDLGELALGQNMRVAFMPW NGYNFEDSILVSERVVQEDRFTTIHIQELACVSRDTKLGP EEITADIPNVGEAALSKLDESGIVYIGAEVTGGDILVGKV TPKGETQLTPEEKLLRAIFGEKASDVKDSSLRVPNGVSGT VIDVQVFTRDGVEKDKRALEIEEMQLKQAKKDLSEELQIL EAGLFSRIRAVLVAGGVEAEKLDKLPRDRWLELGLTDEEK QNQLEQLAEQYDELKHEFEKKLEAKRRKITQGDDLAPGVL KIVKVYLAVKRRIQPGDKMAGRHGNKGVISKINPIEDMPY DENGTPVDIVLNPLGVPSRMNIGQILETHLGMAAKGIGDK INAMLKQQQEVAKLREFIQRAYDLGADVRQKVDLSTFSDE EVMRLAENLRKGMPIATPVFDGAKEAEIKELLKLGDLPTS GQIRLYDGRTGEQFERPVTVGYMYMLKLNHLVDDKMHARS TGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTL QEMLTVKSDDVNGRTKMYKNIVDGNHQMEPGMPESFNVLL KEIRSLGINIELEDE I:  LKAQTKTEEFDAIKIALASPDMIRSWSFGEVKKPETINYR TFKPERDGLFCARIFGPVKDYECLCGKYKRLKHRGVICEK CGVEVTQTKVRRERMGHIELASPTAHIWFLKSLPSRIGLL LDMPLRDIERVLYFESYVVIEGGMTNLERQQILTEEQYLD ALEEFGDEFDAKMGAEAIQALLKSMDLEQECEQLREELNE TNSETKRKKLTKRIKLLEAFVQSGNKPEWMILTVLPVLPP DLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLLDLAA PDIIVRNEKRMLQEAVDALLDNGRRGRAITGSNKRPLKSL ADMIKGGKRVDYSGRSVITVGPYLRLHQCGLPKKMALELF KPFIYGKLELRGLATTIKAAKKMVEREEAVVWDILDEVIR EHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCAAY NADFDGDQMAVHVPLTLEAQLEARALMMSTNNILSPANGE PIIVPSQDVVLGLYYMTRDCVNAKGEGMVLTGPKEAERLY RSGLASLHARVKVRITEYEKDANGELVAKTSLKDTTVGRA ILWMIVPKGLPYSIVNQALGKKAISKMLNTCYRILGLKPT VIFADQIMYTGFAYAARSGASVGIDDMVIPEKKHEIISEA EAEVAEIQEQFQSGLVTAGERYNKVIDIWAAANDRVSKAM MDNLQTETVINRDGQEEKQVSFNSIYMMADSGARGSAAQI RQLAGMRGLMAKPDGSIIETPITANFREGLNVLQYFISTH GARKGLADTALKTANSGYLTRRLVDVAQDLVVTEDDCGTH EGIMMTPVIEGGDVKEPLRDRVLGRVTAEDVLKPGTADIL VPRNTLLHEQWCDLLEENSVDAVKVRSVVSCDTDFGVCAH CYGRDLARGHIINKGEAIGVIAAQSIGEPGTQLTMRDITG GLPRVADLFEARRPKEPAILAEISGIVSFGKETKGKRRLV ITPVDGSDPYEEMIPKWRQLNVFEGERVERGDVISDGPEA PHDILRLRGVHAVTRYIVNEVQDVYRLQGVKINDKHIEVI VRQMLRKATIVNAGSSDFLEGEQVEYSRVKIANRELEANG KVGATYSRDLLGITKASLATESFISAASFQETTRVLTEAA VAGKRDELRGLKENVIVGRLIPAGTGYAYHQDRMRRRAAG J:  ARVTVQDAVEKIGNRFDLVLVAARRARQMQVGGKDPLVPE ENDKTTVIALREIEEGLINNQILDVRERQEQQEQEA X:  QSQLKLLVTRGKEQGYLTYAEVNDHLPEDIVDSDQIEDII QMINDMGIQVMEEAPDADDTDPVRMYMREMGTVELLTREG EIDIAKRIEDGINQVQCSVAEYPEAITYLLEQYDRVEAEI DPELAREKFAELRAQYVVTRDTIKAKGRSHATAQEEILKL SEVFKQFRLVPKQFDYLVNSMRVMMDRVRTQERLIMKLCV EQCKMPKKNFITLFTGNETSDTWFNAAIAMNKPWSEKLHD VSEEVHRALQKLQQIEEETGLTIEQVKDINRRMSIGEAKA RRAKKEMVEANLRLVISIAKKYTNRGLQFLDLIQEGNIGL MKAVDKFEYRRGYKFSTYATWWIRQAITRSIADQARTIRI PVHMIETINKLNRISRQMLQEMGREPTPEELAERMLMPED KIRKVLKIAKEPISMETPIGDDEDSHLGDFIEDTTLELPL DSATTESLRAATHDVLAGLTAREAKVLRMRFGIDMNTDYT LEEVGKQFDVTRERIRQIEAKALRKLRHPSRSEVLRS Y:  TDPVRMYMREMGTVELLTREGEIDIAKRIEDGINQVQCSV AEYPEAITYLLEQYDRVEAEIDPELAREKFAELRAQYVVT RDTIKAKGRSHATAQEEILKLSEVFKQFRLVPKQFDYLVN SMRVMMDRVRTQERLIMKLCVEQCKMPKKNFITLFTGNET SDTWFNAAIAMNKPWSEKLHDVSEEVHRALQKLQQIEEET GLTIEQVKDINRRMSIGEAKARRAKKEMVEANLRLVISIA KKYTNRGLQFLDLIQEGNIGLMKAVDKFEYRRGYKFSTYA TWWIRQAITRSIADQARTIRIPVHMIETINKLNRISRQML QEMGREPTPEELAERMLMPEDKIRKVLKIAKEPISMETPI GDDEDSHLGDFIEDTTLELPLDSATTESLRAATHDVLAGL TAREAKVLRMRFGIDMNTDYTLEEVGKQFDVTRERIRQIE AKALRKLRHPSRSEVLRS Description Functional site 1) chain C residue 510 type sequence Q description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 2) chain C residue 511 type sequence L description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 3) chain C residue 513 type sequence Q description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 4) chain C residue 514 type sequence F description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 5) chain C residue 526 type sequence H description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 6) chain C residue 529 type sequence R description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 7) chain C residue 531 type sequence S description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 8) chain C residue 533 type sequence L description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 9) chain C residue 540 type sequence R description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 10) chain C residue 568 type sequence N description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 11) chain C residue 572 type sequence I description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 12) chain X residue 513 type sequence D description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 13) chain X residue 514 type sequence D description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 14) chain X residue 515 type sequence E description BINDING SITE FOR RESIDUE 1RM C 1401 source : AC1 15) chain D residue 70 type sequence C description BINDING SITE FOR RESIDUE ZN D 1501 source : AC2 16) chain D residue 72 type sequence C description BINDING SITE FOR RESIDUE ZN D 1501 source : AC2 17) chain D residue 85 type sequence C description BINDING SITE FOR RESIDUE ZN D 1501 source : AC2 18) chain D residue 88 type sequence C description BINDING SITE FOR RESIDUE ZN D 1501 source : AC2 19) chain D residue 814 type sequence C description BINDING SITE FOR RESIDUE ZN D 1502 source : AC3 20) chain D residue 888 type sequence C description BINDING SITE FOR RESIDUE ZN D 1502 source : AC3 21) chain D residue 895 type sequence C description BINDING SITE FOR RESIDUE ZN D 1502 source : AC3 22) chain D residue 898 type sequence C description BINDING SITE FOR RESIDUE ZN D 1502 source : AC3 23) chain D residue 462 type sequence D description BINDING SITE FOR RESIDUE MG D 1503 source : AC4 24) chain D residue 464 type sequence D description BINDING SITE FOR RESIDUE MG D 1503 source : AC4 25) chain H residue 509 type sequence S description BINDING SITE FOR RESIDUE 1RM H 1401 source : AC5 26) chain H residue 510 type sequence Q description BINDING SITE FOR RESIDUE 1RM H 1401 source : AC5 27) chain H residue 513 type sequence Q description BINDING SITE FOR RESIDUE 1RM H 1401 source : AC5 28) chain H residue 514 type sequence F description BINDING SITE FOR RESIDUE 1RM H 1401 source : AC5 29) chain H residue 516 type sequence D description BINDING SITE FOR RESIDUE 1RM H 1401 source : AC5 30) chain H residue 526 type sequence H description BINDING SITE FOR RESIDUE 1RM H 1401 source : AC5 31) chain H residue 529 type sequence R description BINDING SITE FOR RESIDUE 1RM H 1401 source : AC5 32) chain H residue 531 type sequence S description BINDING SITE FOR RESIDUE 1RM H 1401 source : AC5 33) chain H residue 533 type sequence L description BINDING SITE FOR RESIDUE 1RM H 1401 source : AC5 34) chain H residue 568 type sequence N description BINDING SITE FOR RESIDUE 1RM H 1401 source : AC5 35) chain H residue 572 type sequence I description BINDING SITE FOR RESIDUE 1RM H 1401 source : AC5 36) chain H residue 687 type sequence R description BINDING SITE FOR RESIDUE 1RM H 1401 source : AC5 37) chain I residue 70 type sequence C description BINDING SITE FOR RESIDUE ZN I 1501 source : AC6 38) chain I residue 72 type sequence C description BINDING SITE FOR RESIDUE ZN I 1501 source : AC6 39) chain I residue 85 type sequence C description BINDING SITE FOR RESIDUE ZN I 1501 source : AC6 40) chain I residue 88 type sequence C description BINDING SITE FOR RESIDUE ZN I 1501 source : AC6 41) chain I residue 814 type sequence C description BINDING SITE FOR RESIDUE ZN I 1502 source : AC7 42) chain I residue 888 type sequence C description BINDING SITE FOR RESIDUE ZN I 1502 source : AC7 43) chain I residue 895 type sequence C description BINDING SITE FOR RESIDUE ZN I 1502 source : AC7 44) chain I residue 898 type sequence C description BINDING SITE FOR RESIDUE ZN I 1502 source : AC7 45) chain I residue 462 type sequence D description BINDING SITE FOR RESIDUE MG I 1503 source : AC8 46) chain I residue 464 type sequence D description BINDING SITE FOR RESIDUE MG I 1503 source : AC8 47) chain D residue 895 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 48) chain D residue 898 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 49) chain I residue 70 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 50) chain I residue 72 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 51) chain I residue 85 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 52) chain I residue 88 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 53) chain I residue 460 type DNA_BIND sequence D description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 54) chain I residue 462 type DNA_BIND sequence D description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 55) chain I residue 464 type DNA_BIND sequence D description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 56) chain I residue 814 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 57) chain I residue 888 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 58) chain I residue 895 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 59) chain I residue 898 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 60) chain D residue 888 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 61) chain X residue 573-592 type DNA_BIND sequence LEEVGKQFDVTRERIRQIEA description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 62) chain Y residue 573-592 type DNA_BIND sequence LEEVGKQFDVTRERIRQIEA description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 63) chain D residue 85 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 64) chain D residue 88 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 65) chain D residue 460 type DNA_BIND sequence D description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 66) chain D residue 462 type DNA_BIND sequence D description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 67) chain D residue 464 type DNA_BIND sequence D description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 68) chain D residue 814 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 69) chain A residue 298 type MOD_RES sequence K description N6-acetyllysine; by PatZ => ECO:0000269|PubMed:21696463 source Swiss-Prot : SWS_FT_FI3 70) chain C residue 1063-1075 type prosite sequence GDKMAGRHGNKGV description RNA_POL_BETA RNA polymerases beta chain signature. GdKMAGrHGNKGV source prosite : PS01166 71) chain X residue 403-416 type prosite sequence DLIQEGNIGLMKAV description SIGMA70_1 Sigma-70 factors family signature 1. DLIQeGnIGLMkAV source prosite : PS00715 72) chain X residue 572-598 type prosite sequence TLEEVGKQFDVTRERIRQIEAKALRKL description SIGMA70_2 Sigma-70 factors family signature 2. TleEVGkqfdVTrerIrQIEakaLrkL source prosite : PS00716 73) chain Y residue 562 type SITE sequence R description Interaction with anti-sigma factors source Swiss-Prot : SWS_FT_FI2 74) chain X residue 562 type SITE sequence R description Interaction with anti-sigma factors source Swiss-Prot : SWS_FT_FI2

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