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Database: UniProt
Entry: A0A097QZK0_HAFAL
LinkDB: A0A097QZK0_HAFAL
Original site: A0A097QZK0_HAFAL 
ID   A0A097QZK0_HAFAL        Unreviewed;       432 AA.
AC   A0A097QZK0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Peptidase B {ECO:0000256|HAMAP-Rule:MF_00504};
DE            EC=3.4.11.23 {ECO:0000256|HAMAP-Rule:MF_00504};
DE   AltName: Full=Aminopeptidase B {ECO:0000256|HAMAP-Rule:MF_00504};
GN   Name=pepB {ECO:0000256|HAMAP-Rule:MF_00504};
GN   ORFNames=AT03_05360 {ECO:0000313|EMBL:AIU71870.1};
OS   Hafnia alvei FB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Hafnia.
OX   NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU71870.1, ECO:0000313|Proteomes:UP000029986};
RN   [1] {ECO:0000313|EMBL:AIU71870.1, ECO:0000313|Proteomes:UP000029986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB1 {ECO:0000313|EMBL:AIU71870.1,
RC   ECO:0000313|Proteomes:UP000029986};
RX   PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA   Tan J.Y., Yin W.F., Chan K.G.;
RT   "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT   pathogenesis: a draft genome perspective.";
RL   Gut Pathog. 6:29-29(2014).
CC   -!- FUNCTION: Probably plays an important role in intracellular peptide
CC       degradation. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00504};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00504};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00504};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00504}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00504}.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528, ECO:0000256|HAMAP-Rule:MF_00504}.
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DR   EMBL; CP009706; AIU71870.1; -; Genomic_DNA.
DR   RefSeq; WP_025800423.1; NZ_CP009706.1.
DR   AlphaFoldDB; A0A097QZK0; -.
DR   MEROPS; M17.004; -.
DR   GeneID; 56890615; -.
DR   KEGG; hav:AT03_05360; -.
DR   PATRIC; fig|1453496.5.peg.1065; -.
DR   eggNOG; COG0260; Bacteria.
DR   HOGENOM; CLU_013734_7_1_6; -.
DR   OrthoDB; 9809354at2; -.
DR   Proteomes; UP000029986; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP-
KW   Rule:MF_00504};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00504};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00504};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00504};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00504};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00504};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029986}.
FT   DOMAIN          276..283
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
FT   ACT_SITE        208
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT   BINDING         196
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT   BINDING         201
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT   BINDING         201
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT   BINDING         219
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT   BINDING         278
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT   BINDING         280
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT   BINDING         280
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
SQ   SEQUENCE   432 AA;  46513 MW;  74C55B2696492B75 CRC64;
     MSTEFMPVSL SHQPADARWG EKALLSSGSE GMVIHLNGNG ELVAVQRAAR KLDGQGIKQV
     HLAGEGWDLE KCWAFWQGYR GPKGSRQVQW PDLSESDRAE LDRRLKIVDW VRDTINAPAE
     EVGPSQLAQR AVDLMCSVAC DNVSYRITKG EDLREQGYMG LHTVGRGSER SPVLLALDYN
     PTGNPDAPVL ACLVGKGITF DSGGYSMKQS AFMDSMKSDM GGAATVTGAL ALAVSRGLNQ
     RVKLYLCCAD NLVSGNAFKL GDIITYRNGK TVEIMNTDAE GRLVLADGLI DASEQNAAMI
     IDCATLTGAA KTALGNDYHA LFSFDDALAA DMLQSAEQEN EAFWRLPLAE FHRSQLPSNF
     AELNNVAGAA YGAGASTAAA FLSYFVKEYR QGWLHIDCSA TYRKSAVDQW AAGATGLGVR
     ALANLLLEKA KA
//
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