HTPX_ECOBW
ID HTPX_ECOBW Reviewed; 293 AA.
AC C4ZZI6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=BWG_1643;
OS Escherichia coli (strain K12 / MC4100 / BW2952).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=595496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MC4100 / BW2952;
RX PubMed=19376874; DOI=10.1128/jb.00118-09;
RA Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA Wang L.;
RT "Genomic sequencing reveals regulatory mutations and recombinational events
RT in the widely used MC4100 lineage of Escherichia coli K-12.";
RL J. Bacteriol. 191:4025-4029(2009).
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; CP001396; ACR64344.1; -; Genomic_DNA.
DR RefSeq; WP_000984520.1; NC_012759.1.
DR AlphaFoldDB; C4ZZI6; -.
DR SMR; C4ZZI6; -.
DR MEROPS; M48.002; -.
DR KEGG; ebw:BWG_1643; -.
DR HOGENOM; CLU_042266_1_0_6; -.
DR OMA; AVCCTEG; -.
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; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..293
FT /note="Protease HtpX"
FT /id="PRO_1000203973"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 158..178
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 140
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 143
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; 31923 MW; 13253716D92DD5BF CRC64;
MMRIALFLLT NLAVMVVFGL VLSLTGIQSS SVQGLMIMAL LFGFGGSFVS LLMSKWMALR
SVGGEVIEQP RNERERWLVN TVATQARQAG IAMPQVAIYH APDINAFATG ARRDASLVAV
STGLLQNMSP DEAEAVIAHE ISHIANGDMV TMTLIQGVVN TFVIFISRIL AQLAAGFMGG
NRDEGEESNG NPLIYFAVAT VLELVFGILA SIITMWFSRH REFHADAGSA KLVGREKMIA
ALQRLKTSYE PQEATSMMAL CINGKSKSLS ELFMTHPPLD KRIEALRTGE YLK
