ID   HTPX_CELJU              Reviewed;         293 AA.
AC   B3PJ06;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Protease HtpX {ECO:0000255|HAMAP-Rule:MF_00188};
DE            EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_00188};
DE   AltName: Full=Heat shock protein HtpX {ECO:0000255|HAMAP-Rule:MF_00188};
GN   Name=htpX {ECO:0000255|HAMAP-Rule:MF_00188}; OrderedLocusNames=CJA_0517;
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107;
RX   PubMed=18556790; DOI=10.1128/jb.01701-07;
RA   DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
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}.
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DR   EMBL; CP000934; ACE83478.1; -; Genomic_DNA.
DR   RefSeq; WP_012486197.1; NC_010995.1.
DR   AlphaFoldDB; B3PJ06; -.
DR   SMR; B3PJ06; -.
DR   STRING; 498211.CJA_0517; -.
DR   PRIDE; B3PJ06; -.
DR   EnsemblBacteria; ACE83478; ACE83478; CJA_0517.
DR   KEGG; cja:CJA_0517; -.
DR   eggNOG; COG0501; Bacteria.
DR   HOGENOM; CLU_042266_1_0_6; -.
DR   OMA; AVCCTEG; -.
DR   OrthoDB; 1918093at2; -.
DR   Proteomes; UP000001036; Chromosome.
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.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Stress response;
KW   Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..293
FT                   /note="Protease HtpX"
FT                   /id="PRO_1000098813"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         149
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   293 AA;  31698 MW;  F8E9C8D14BA6ACDD CRC64;
     MLRIGLFLLT NLAVLVVAGV VLSLLGVGNY RTADGLDLTN LLIFCAVFGF VGSFISLFLS
     KWMAKKTMGV QLIEQPRNAD EKWLVDTVVE LSQKAGIKTP EIGVFAAQES NAFATGWNRN
     DALVAVSLGL LQRFERDEVK AVLAHEIGHV ANGDMITLSL IQGVVNTFVM FFARIIGDLV
     DRVIFKNEEG RGIAFFITTI VAELVLGILA SMIVAAFSRY REYRADAAGA TLADRGAMIR
     ALQRLQAEMS AGVESPLPSS MRAFGISGGV RNLFASHPPL EARIQALRDS AHG