eF-site ID 6fms-A PDB Code 6fms Chain A click to enlarge Title IMISX-EP of Se-LspA Classification HYDROLASE Compound Lipoprotein signal peptidase Source (6FMS) Sequence A:  PDVDRFGRLPWLWITVLVFVLDQVSKAFFQAELSXYQQIV VIPDLFSWTLAYNTGAAFSFLADSSGWQRWLFALIAIVVS ASLVVWLKRLKKGETWLAIALALVLGGALGNLYDRXVLGH VVDFILVHWQNRWYFPAFNLADSAITVGAVXLALDXF Description Functional site 1) chain A residue 29 type sequence F description binding site for residue OLC A 201 source : AC1 2) chain A residue 40 type sequence I description binding site for residue OLC A 201 source : AC1 3) chain A residue 42 type sequence V description binding site for residue OLC A 202 source : AC2 4) chain A residue 49 type sequence W description binding site for residue OLC A 202 source : AC2 5) chain A residue 11 type sequence P description binding site for residue OLC A 203 source : AC3 6) chain A residue 12 type sequence W description binding site for residue OLC A 203 source : AC3 7) chain A residue 15 type sequence I description binding site for residue OLC A 203 source : AC3 8) chain A residue 7 type sequence F description binding site for residue OLC A 204 source : AC4 9) chain A residue 10 type sequence L description binding site for residue OLC A 204 source : AC4 10) chain A residue 11 type sequence P description binding site for residue OLC A 204 source : AC4 11) chain A residue 14 type sequence W description binding site for residue OLC A 204 source : AC4 12) chain A residue 70 type sequence R description binding site for residue OLC A 205 source : AC5 13) chain A residue 117 type sequence X description binding site for residue OLC A 205 source : AC5 14) chain A residue 63 type sequence A description binding site for residue OLC B 204 source : AC8 15) chain A residue 64 type sequence D description binding site for residue OLC B 204 source : AC8 16) chain A residue 139 type sequence F description binding site for residue OLC E 301 source : AD9 17) chain A residue 143 type sequence D description binding site for residue OLC E 301 source : AD9 18) chain A residue 148 type sequence V description binding site for residue OLC E 301 source : AD9 19) chain A residue 54 type sequence N description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203 source : AE3 20) chain A residue 56 type sequence G description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203 source : AE3 21) chain A residue 59 type sequence F description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203 source : AE3 22) chain A residue 73 type sequence F description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203 source : AE3 23) chain A residue 112 type sequence N description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203 source : AE3 24) chain A residue 116 type sequence R description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203 source : AE3 25) chain A residue 124 type sequence D description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203 source : AE3 26) chain A residue 143 type sequence D description binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203 source : AE3 27) chain A residue 105-117 type prosite sequence VLGGALGNLYDRX description SPASE_II Signal peptidases II signature. VlGGALGNLYDRM source prosite : PS00855 28) chain A residue 68-89 type TRANSMEM sequence WQRWLFALIAIVVSASLVVWLK description Helical => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS source Swiss-Prot : SWS_FT_FI3 29) chain A residue 97-118 type TRANSMEM sequence WLAIALALVLGGALGNLYDRXV description Helical => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS source Swiss-Prot : SWS_FT_FI3 30) chain A residue 90-96 type TOPO_DOM sequence RLKKGET description Cytoplasmic => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS source Swiss-Prot : SWS_FT_FI4 31) chain A residue 141-154 type TRANSMEM sequence LADSAITVGAVXLA description Helical => ECO:0000269|PubMed:26912896, ECO:0007744|PDB:5DIR source Swiss-Prot : SWS_FT_FI5 32) chain A residue 124 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000305|PubMed:26912896 source Swiss-Prot : SWS_FT_FI7 33) chain A residue 143 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000305|PubMed:26912896 source Swiss-Prot : SWS_FT_FI7 34) chain A residue 10-30 type TRANSMEM sequence LPWLWITVLVFVLDQVSKAFF description Helical => ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS source Swiss-Prot : SWS_FT_FI1 35) chain A residue 31-67 type TOPO_DOM sequence QAELSXYQQIVVIPDLFSWTLAYNTGAAFSFLADSSG description Periplasmic => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS source Swiss-Prot : SWS_FT_FI2 36) chain A residue 119-140 type TOPO_DOM sequence LGHVVDFILVHWQNRWYFPAFN description Periplasmic => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS source Swiss-Prot : SWS_FT_FI2

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