Y1156_BRUSU
ID Y1156_BRUSU Reviewed; 379 AA.
AC Q8G0E1; G0KA78;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Putative zinc metalloprotease BR1156/BS1330_I1152;
DE EC=3.4.24.-;
GN OrderedLocusNames=BR1156, BS1330_I1152;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AE014291; AAN30076.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18494.1; -; Genomic_DNA.
DR RefSeq; WP_002966847.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8G0E1; -.
DR SMR; Q8G0E1; -.
DR PRIDE; Q8G0E1; -.
DR EnsemblBacteria; AEM18494; AEM18494; BS1330_I1152.
DR GeneID; 45052197; -.
DR GeneID; 55590837; -.
DR KEGG; bms:BR1156; -.
DR KEGG; bsi:BS1330_I1152; -.
DR PATRIC; fig|204722.21.peg.1960; -.
DR HOGENOM; CLU_025778_1_0_5; -.
DR OMA; QYMVGFG; -.
DR PhylomeDB; Q8G0E1; -.
DR Proteomes; UP000007104; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR TIGRFAMs; TIGR00054; TIGR00054; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..379
FT /note="Putative zinc metalloprotease BR1156/BS1330_I1152"
FT /id="PRO_0000088433"
FT TRANSMEM 39..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 133..208
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 34
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 379 AA; 40934 MW; 9713A92F8A436310 CRC64;
MQEALALFFG SESLLVGTII PFLFVLTVVV FVHEMGHYLV ARWCGIGAQA FSIGFGPELL
GFTDRHGTRW KLSAIPLGGY VKFIGDESET SSPVGVNESA LSEEDRKRAF HTQPVWKRAA
TVFAGPAFNI ILTIAIFSVF FALYGRQIAD PLIAGVQPGS PAAEAGFEPG DRFVSVEGEK
ITTFADVQRI VSGRAGDKLN FTVERDGKMV DLQAVPKIVE RTDPLGNKVK LGAIGVETTE
AVGNFRRIEY GPLESVGQAV IETGHIIGRT GEFFKRFAVG REDKCQLGGP VKIATMASKA
ASQGFDWLIQ LMAMLSIGIG LLNLFPLPPL DGGHLVFYAV EAIKGSPVSG AAQEIFYRIG
FLLVMGFMGF VLFNDLFAC
