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
//