eF-site ID 6hrb-B PDB Code 6hrb Chain B click to enlarge Title Cryo-EM structure of the KdpFABC complex in an E2 inward-facing state (state 2) Classification MEMBRANE PROTEIN Compound Potassium-transporting ATPase potassium-binding subunit Source (KDPF_ECOLI) Sequence B:  FEPTLVVQALKEAVKKLNPQAQWRNPVMFIVWIGSLLTTC ISIAMASGAMPGNALFSAAISGWLWITVLFANFAEALAEG RSKAQANSLKGVKKTAFARKLREPKYGAAADKVPADQLRK GDIVLVEAGDIIPCDGEVIEGGASVDESAITGEXAPVIRE SGGDFASVTGGTRILSDWLVIECSVNPGETFLDRMIAMVE GAQRRKTPNEIALTILLIALTIVFLLATATLWPFSAWGGN AVSVTVLVALLVCLIPTTIGGLLSAIGVAGMSRMLGANVI ATSGRAVEAAGDVDVLLLDKTGTITLGNRQASEFIPAQGV DEKTLADAAQLASLADETPEGRSIVILAKQRFNLRERDVQ SLHATFVPFTAQSRMSGINIDNRMIRKGSVDAIRRHVEAN GGHFPTDVDQKVDQVARQGATPLVVVEGSRVLGVIALKDI VKGGIKERFAQLRKMGIKTVMITGDNRLTAAAIAAEAGVD DFLAEATPEAKLALIRQYQAEGRLVAMTGDGTNDAPALAQ ADVAVAMNSGTQAAKEAGNMVDLDSNPTKLIEVVHIGKQM LMTRGSLTTFSIANDVAKYFAIIPAAFAATYPQLNALNIM CLHSPDSAILSAVIFNALIIVFLIPLALKGVSYKPLTASA MLRRNLWIYGLGGLLVPFIGIKVIDLLLTVCGLV Description (1)  Potassium-transporting ATPase potassium-binding subunit, Potassium-transporting ATPase ATP-binding subunit (E.C.3.6.3.12), Potassium-transporting ATPase KdpC subunit, Potassium-transporting ATPase KdpF subunit Functional site 1) chain B residue 81-222 type TOPO_DOM sequence FAEALAEGRSKAQANSLKGVKKTAFARKLREPKYGAAADK VPADQLRKGDIVLVEAGDIIPCDGEVIEGGASVDESAITG EXAPVIRESGGDFASVTGGTRILSDWLVIECSVNPGETFL DRMIAMVEGAQRRKTPNEIALT description Periplasmic => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378 source Swiss-Prot : SWS_FT_FI1 2) chain B residue 264-574 type TOPO_DOM sequence PTTIGGLLSAIGVAGMSRMLGANVIATSGRAVEAAGDVDV LLLDKTGTITLGNRQASEFIPAQGVDEKTLADAAQLASLA DETPEGRSIVILAKQRFNLRERDVQSLHATFVPFTAQSRM SGINIDNRMIRKGSVDAIRRHVEANGGHFPTDVDQKVDQV ARQGATPLVVVEGSRVLGVIALKDIVKGGIKERFAQLRKM GIKTVMITGDNRLTAAAIAAEAGVDDFLAEATPEAKLALI RQYQAEGRLVAMTGDGTNDAPALAQADVAVAMNSGTQAAK EAGNMVDLDSNPTKLIEVVHIGKQMLMTRGS description Periplasmic => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378 source Swiss-Prot : SWS_FT_FI1 3) chain B residue 632-653 type TOPO_DOM sequence IPLALKGVSYKPLTASAMLRRN description Periplasmic => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378 source Swiss-Prot : SWS_FT_FI1 4) chain B residue 62-80 type TRANSMEM sequence ALFSAAISGWLWITVLFAN description Helical => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378, ECO:0007744|PDB:5MRW, ECO:0007744|PDB:6HRA source Swiss-Prot : SWS_FT_FI2 5) chain B residue 223-242 type TRANSMEM sequence ILLIALTIVFLLATATLWPF description Helical => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378, ECO:0007744|PDB:5MRW, ECO:0007744|PDB:6HRA source Swiss-Prot : SWS_FT_FI2 6) chain B residue 252-263 type TRANSMEM sequence VTVLVALLVCLI description Helical => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378, ECO:0007744|PDB:5MRW, ECO:0007744|PDB:6HRA source Swiss-Prot : SWS_FT_FI2 7) chain B residue 575-595 type TRANSMEM sequence LTTFSIANDVAKYFAIIPAAF description Helical => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378, ECO:0007744|PDB:5MRW, ECO:0007744|PDB:6HRA source Swiss-Prot : SWS_FT_FI2 8) chain B residue 613-631 type TRANSMEM sequence PDSAILSAVIFNALIIVFL description Helical => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378, ECO:0007744|PDB:5MRW, ECO:0007744|PDB:6HRA source Swiss-Prot : SWS_FT_FI2 9) chain B residue 654-678 type TRANSMEM sequence LWIYGLGGLLVPFIGIKVIDLLLTV description Helical => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378, ECO:0007744|PDB:5MRW, ECO:0007744|PDB:6HRA source Swiss-Prot : SWS_FT_FI2 10) chain B residue 243-251 type TOPO_DOM sequence SAWGGNAVS description Cytoplasmic => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378 source Swiss-Prot : SWS_FT_FI3 11) chain B residue 596-612 type TOPO_DOM sequence AATYPQLNALNIMCLHS description Cytoplasmic => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378 source Swiss-Prot : SWS_FT_FI3 12) chain B residue 679-682 type TOPO_DOM sequence CGLV description Cytoplasmic => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 307 type ACT_SITE sequence D description 4-aspartylphosphate intermediate => ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:1474895 source Swiss-Prot : SWS_FT_FI4 14) chain B residue 344 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:16354672, ECO:0007744|PDB:2A00, ECO:0007744|PDB:2A29 source Swiss-Prot : SWS_FT_FI5 15) chain B residue 377 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:16354672, ECO:0007744|PDB:2A00, ECO:0007744|PDB:2A29 source Swiss-Prot : SWS_FT_FI5 16) chain B residue 395 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:16354672, ECO:0007744|PDB:2A00, ECO:0007744|PDB:2A29 source Swiss-Prot : SWS_FT_FI5 17) chain B residue 348 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:16354672, ECO:0007744|PDB:2A00 source Swiss-Prot : SWS_FT_FI6 18) chain B residue 307-313 type prosite sequence DKTGTIT description ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTIT source prosite : PS00154 19) chain B residue 518 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00285 source Swiss-Prot : SWS_FT_FI7 20) chain B residue 522 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00285 source Swiss-Prot : SWS_FT_FI7 21) chain B residue 162 type MOD_RES sequence X description Phosphoserine => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378 source Swiss-Prot : SWS_FT_FI8

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