ID   A9MAB0_BRUC2            Unreviewed;       460 AA.
AC   A9MAB0;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Peptidase B {ECO:0000313|EMBL:ABX63205.1};
GN   Name=pepB {ECO:0000313|EMBL:ABX63205.1};
GN   OrderedLocusNames=BCAN_A2223 {ECO:0000313|EMBL:ABX63205.1};
OS   Brucella canis (strain ATCC 23365 / NCTC 10854).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=483179 {ECO:0000313|EMBL:ABX63205.1, ECO:0000313|Proteomes:UP000001385};
RN   [1] {ECO:0000313|EMBL:ABX63205.1, ECO:0000313|Proteomes:UP000001385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23365 / NCTC 10854 {ECO:0000313|Proteomes:UP000001385};
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA   Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA   Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA   Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA   Bruce D., Detter C., Munk C., Brettin T.S.;
RT   "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   EMBL; CP000872; ABX63205.1; -; Genomic_DNA.
DR   RefSeq; WP_006133040.1; NC_010103.1.
DR   AlphaFoldDB; A9MAB0; -.
DR   GeneID; 55591742; -.
DR   KEGG; bcs:BCAN_A2223; -.
DR   HOGENOM; CLU_013734_2_1_5; -.
DR   PhylomeDB; A9MAB0; -.
DR   Proteomes; UP000001385; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   InterPro; IPR048816; Peptidase_M17_N_1.
DR   PANTHER; PTHR11963:SF53; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF21337; Peptidase_M17_N_1; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          306..313
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   460 AA;  48729 MW;  A05BDF8CBEB16369 CRC64;
     MSAEIISQKS AASRPIWFVA KNALDEAALP ESAAAWAKAN GFDGEAGRVL VLPGRDGAIA
     GALFGTGEAP ENGQPQLIAG KLARNLPEGD WHIEGKPGDA GLAALAFLMG GYSFTRYRKA
     NGKTVRLALP EGADASETRR LAEAVTLVRD LINTPANDMG PAALEQAARD LAAQHGARVA
     TTEGEALLEK NFPMIHAVGR AGAVAPRLID LQWGRDSDPK ITLVGKGVCF NTGGLDIKSA
     SGMLLMKKDM GGAANVLGLA ALIMDAKLPV RLRVLIPAVE NAIAGNAFRP GDILQSRKGL
     TVEIGNTDAE GRLVLADALA LADEEEPEML IDMATLTGAA RVALGPDLPP FYTHDDQLAG
     EIAVKARETA DPLWRMPLWQ PYAQKLSSRV ADINNVTTDG FAGSVTAALF LAKFVERARQ
     WAHFDIFGWV PVEKPASPVG GEAQAIRALY QLLKERYPAR
//