ID   Y829_BRUME              Reviewed;         379 AA.
AC   Q8YHH1;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Putative zinc metalloprotease BMEI0829;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=BMEI0829;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008917; AAL52010.1; -; Genomic_DNA.
DR   PIR; AG3355; AG3355.
DR   RefSeq; WP_004683868.1; NZ_GG703780.1.
DR   AlphaFoldDB; Q8YHH1; -.
DR   SMR; Q8YHH1; -.
DR   STRING; 224914.BMEI0829; -.
DR   EnsemblBacteria; AAL52010; AAL52010; BMEI0829.
DR   GeneID; 29593638; -.
DR   KEGG; bme:BMEI0829; -.
DR   PATRIC; fig|224914.52.peg.616; -.
DR   eggNOG; COG0750; Bacteria.
DR   OMA; QYMVGFG; -.
DR   PhylomeDB; Q8YHH1; -.
DR   Proteomes; UP000000419; 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 BMEI0829"
FT                   /id="PRO_0000088432"
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;  40977 MW;  E6C5A34230273704 CRC64;
     MQEALALFFG SESLLVGTII PFLFVLTVVV FVHEMGHYLV ARWCGIGAQA FSIGFGPELL
     GFTDRHGTRW KLSAIPLVGY 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