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Database: UniProt
Entry: D7H534_BRUAO
LinkDB: D7H534_BRUAO
Original site: D7H534_BRUAO 
ID   D7H534_BRUAO            Unreviewed;       483 AA.
AC   D7H534;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Protease {ECO:0000313|EMBL:EFH33136.1};
GN   ORFNames=BAYG_02677 {ECO:0000313|EMBL:EFH33136.1};
OS   Brucella abortus bv. 5 str. B3196.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=520453 {ECO:0000313|EMBL:EFH33136.1, ECO:0000313|Proteomes:UP000005752};
RN   [1] {ECO:0000313|EMBL:EFH33136.1, ECO:0000313|Proteomes:UP000005752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B3196 {ECO:0000313|EMBL:EFH33136.1,
RC   ECO:0000313|Proteomes:UP000005752};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Ward D., Whatmore A.M., Perrett L.L., O'Callaghan D., Young S., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Brucella abortus bv. 5 str. B3196.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; GG774528; EFH33136.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7H534; -.
DR   HOGENOM; CLU_009902_1_0_5; -.
DR   Proteomes; UP000005752; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EFH33136.1};
KW   Protease {ECO:0000313|EMBL:EFH33136.1}.
FT   DOMAIN          45..190
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          199..387
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          454..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  53007 MW;  32E473A3A3AAFB8A CRC64;
     MQPAAPAETQ PAPAAPAAPV AQAALPEIFR LDGVSNFTLP NGMQVVVIPD HRAPVVTQMV
     WYHVGAADEA PGVSGIAHFL EHLMFKGTKN HPAGEFSARI ASIGGQENAF TSYDYTAYFQ
     RVSPEALEMV MDFESDRMEN LVLDEEAVKT EREVILEERR MRIDSNPGAM LMENTDAVLF
     YNHPYRKPVI GWQQEMEKLS LKNAIDFYNQ YYTPNNATLV IAGDVTPERV RELAMKTWAN
     VHKRAEVLLR ERPQEPAKHA ARVVTLHDER VSTPSFRISW LVPSYANEKR FANAKPGDAP
     ALDLLSEILG GSQLSQLYQQ LIVKQGIAAE TGASYDGDAL DDGTFSVYGV PRNGASLGDV
     EKAVAAQVDR IIRDGVTQAE LDQARNRFLK AVIFARDSQT GMARIYGSAL SVGQTVDDIQ
     KWPDLIKSVT VDQIKDVARR YLVKDQAVTS YLLPPDTEAE SARKKPNAPA NDASASGAGG
     AIQ
//
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