ID   I3D814_9PAST            Unreviewed;       436 AA.
AC   I3D814;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Peptidase B {ECO:0000313|EMBL:EIJ67857.1};
DE            EC=3.4.11.23 {ECO:0000313|EMBL:EIJ67857.1};
GN   Name=pepB {ECO:0000313|EMBL:EIJ67857.1};
GN   ORFNames=HMPREF1052_0573 {ECO:0000313|EMBL:EIJ67857.1};
OS   Pasteurella bettyae CCUG 2042.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=1095749 {ECO:0000313|EMBL:EIJ67857.1, ECO:0000313|Proteomes:UP000006457};
RN   [1] {ECO:0000313|EMBL:EIJ67857.1, ECO:0000313|Proteomes:UP000006457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 2042 {ECO:0000313|EMBL:EIJ67857.1,
RC   ECO:0000313|Proteomes:UP000006457};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIJ67857.1}.
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DR   EMBL; AJSX01000041; EIJ67857.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3D814; -.
DR   MEROPS; M17.004; -.
DR   PATRIC; fig|1095749.3.peg.1872; -.
DR   eggNOG; COG0260; Bacteria.
DR   Proteomes; UP000006457; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00433; Peptidase_M17; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 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,
KW   ECO:0000313|EMBL:EIJ67857.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EIJ67857.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006457}.
FT   DOMAIN          279..286
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   436 AA;  47531 MW;  C8578A47DA1A3C76 CRC64;
     MIMKINLSTE QASEIWGKNA LISFANEQAT IHLKNNEKSD RTLVQTAARK LRTQGINDVE
     LIGYDWNLEY CWAFYQGFYT AKQDWAVEFP ELGEDHEELL ARINAGDFVR EIVNLPADVI
     TPVVLANRAA QFISDLAEQY ADKSAVSFRI ISGKELREQN YLGLWNVGKG SVNPPAMLQL
     DYNPTGNPDA PVLACLVGKG ITFDSGGYSI KPSNFMDSMR SDMGGAALVT GGLGLAIARG
     LNQRVKLYLC CAENLVSSTA FKLGDIIEYR NGVTVEILNT DAEGRLVLAD GLIDASEQQA
     GFILDAATLT GAAKVAVGND YHSVLSMDDH LVNELLDSAK EEFEPFWRLP FEEFHRSQVS
     SSFADISNTA SVAVAAGAST ATAFLSKFVK SYDKNWLHLD CSATFRKTPS ELWATGATGL
     GVQTIANLLV TKATQI
//