PEPB_HAEIN
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 03-AUG-2022, entry version 105.
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}; OrderedLocusNames=HI_0875;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; 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;
CC Evidence={ECO:0000255|HAMAP-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};
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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:0004177; F:aminopeptidase activity; 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:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR HAMAP; MF_00504; Aminopeptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR008330; Pept_M17_PepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF12404; DUF3663; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PIRSF; PIRSF036388; Ctsl_amnpptdse_B; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
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
