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
//