ID   HTPX_BRUAB              Reviewed;         325 AA.
AC   Q57B74;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Protease HtpX homolog {ECO:0000255|HAMAP-Rule:MF_00188};
DE            EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_00188};
GN   Name=htpX {ECO:0000255|HAMAP-Rule:MF_00188}; OrderedLocusNames=BruAb1_1793;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00188};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00188};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00188}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00188}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000255|HAMAP-
CC       Rule:MF_00188}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017223; AAX75110.1; -; Genomic_DNA.
DR   RefSeq; WP_002964890.1; NC_006932.1.
DR   AlphaFoldDB; Q57B74; -.
DR   EnsemblBacteria; AAX75110; AAX75110; BruAb1_1793.
DR   GeneID; 3788759; -.
DR   KEGG; bmb:BruAb1_1793; -.
DR   HOGENOM; CLU_042266_3_0_5; -.
DR   OMA; AVCCTEG; -.
DR   Proteomes; UP000000540; 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:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   HAMAP; MF_00188; Pept_M48_protease_HtpX; 1.
DR   InterPro; IPR022919; Pept_M48_protease_HtpX.
DR   InterPro; IPR001915; Peptidase_M48.
DR   Pfam; PF01435; Peptidase_M48; 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..325
FT                   /note="Protease HtpX homolog"
FT                   /id="PRO_1000077444"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   REGION          288..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   325 AA;  34500 MW;  BB5159B8E1B030E5 CRC64;
     MNMTKTAMLI ALMTVMFMSI GYLLGGGGGM MIALVIAVAM NLFGYWNSDK MVLRMYNAQE
     VDERSAPEYY RMVSGLAANA GLPMPKVYII HEDQPNAFAT GRNPENAAVA ATTGLLNRLS
     PEEVAGVMAH ELAHVQNRDT LTMTIVATLA GAISMLGNFA FFLGGNRENG NGVMGVVGTL
     LAMIVAPFGA MIVQMAVSRT REYAADKRGA EICGNPLWLS SALGRIARGA KVIPNEEAEH
     NPATAHMFII NPLSGRGADN LFSTHPDTDN RIAALEQMAA EMGIRSAAMT ARAAAPSQNS
     GPWGQRSDNA GGNSNGGSRY RGPWS