ID PEPB_HAEIN Reviewed; 434 AA. AC P58474; DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 13-DEC-2001, sequence version 1. DT 13-SEP-2023, entry version 110. DE RecName: Full=Putative peptidase B; DE EC=3.4.11.23 {ECO:0000255|HAMAP-Rule:MF_00504}; DE AltName: Full=Aminopeptidase B {ECO:0000255|HAMAP-Rule:MF_00504}; GN Name=pepB {ECO:0000255|HAMAP-Rule:MF_00504}; GN OrderedLocusNames=HI_0875; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probably plays an important role in intracellular peptide CC degradation. {ECO:0000255|HAMAP-Rule:MF_00504}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal amino acid, Xaa, from a peptide or CC arylamide. Xaa is preferably Glu or Asp but may be other amino acids, CC including Leu, Met, His, Cys and Gln.; EC=3.4.11.23; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00504}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00504}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00504}; CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00504}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00504}. CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000255|HAMAP- CC Rule:MF_00504}. CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=L42023; Type=Frameshift; Note=This may be a natural frameshift.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; P58474; -. DR SMR; P58474; -. DR MEROPS; M17.004; -. DR PhylomeDB; P58474; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro. DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR CDD; cd00433; Peptidase_M17; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR HAMAP; MF_00504; Aminopeptidase_M17; 1. DR InterPro; IPR011356; Leucine_aapep/pepB. DR InterPro; IPR047620; M17_PepB-like_N. DR InterPro; IPR008330; Pept_M17_PepB. DR InterPro; IPR000819; Peptidase_M17_C. DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1. DR PANTHER; PTHR11963:SF20; PEPTIDASE B; 1. DR Pfam; PF12404; DUF3663; 1. DR Pfam; PF00883; Peptidase_M17; 1. DR PIRSF; PIRSF036388; Ctsl_amnpptdse_B; 1. DR PRINTS; PR00481; LAMNOPPTDASE. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. DR PROSITE; PS00631; CYTOSOL_AP; 1. PE 5: Uncertain; KW Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease; KW Reference proteome. FT CHAIN 1..434 FT /note="Putative peptidase B" FT /id="PRO_0000165836" FT ACT_SITE 210 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504" FT ACT_SITE 284 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504" FT BINDING 198 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504" FT BINDING 203 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504" FT BINDING 203 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504" FT BINDING 221 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504" FT BINDING 280 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504" FT BINDING 282 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504" FT BINDING 282 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504" SQ SEQUENCE 434 AA; 47285 MW; A5A592E51EB18B58 CRC64; MQITLSNTLA NDAWGKNAIL SFDSNKAMIH LKNNGKTDRT LVQQAARKLR GQGIKEVELV GEKWDLEFCW AFYQGFYTAK QDYAIEFPHL DDEPQDELLA RIECGDFVRG IINEPAQSLT PVKLVERAAE FILNQADIYN EKSAVSFKII SGEELEQQGY HGIWTVGKGS ANLPAMLQLD FNPTQDSNAP VLACLVGKGI TFDSGGYSIK PSDGMSTMRT DMGGAALLTG ALGFAIARGL NQRVKLYLCC AENLVSNNAF KLGDIITYKN GVSAEVLNTD AEGRLVLADG LIEADNQNPG FIIDCATLTG AAKSAVGNDY HSVLSMDDEL VKNLFQSAQA ENEPFWRLPF EDFHRSQINS SFADIANIGS VPVGAGASTA TAFLSYFVKN YKQNWLHIDC SATYRKSGSD LWSVGATGIG VQTLANLMLS RSLK //