HTPX_VIBPA
ID HTPX_VIBPA Reviewed; 287 AA.
AC Q87QN1;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=VP1118;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 58-161.
RG Midwest center for structural genomics (MCSG);
RT "The crystal structure of heat shock protein Htpx domain from Vibrio
RT parahaemolyticus RIMD 2210633.";
RL Submitted (FEB-2009) to the PDB data bank.
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; BA000031; BAC59381.1; -; Genomic_DNA.
DR RefSeq; NP_797497.1; NC_004603.1.
DR RefSeq; WP_005459987.1; NC_004603.1.
DR PDB; 3CQB; X-ray; 1.86 A; A/B=58-161.
DR PDBsum; 3CQB; -.
DR AlphaFoldDB; Q87QN1; -.
DR SMR; Q87QN1; -.
DR STRING; 223926.28806105; -.
DR MEROPS; M09.001; -.
DR MEROPS; M48.002; -.
DR EnsemblBacteria; BAC59381; BAC59381; BAC59381.
DR GeneID; 1188623; -.
DR KEGG; vpa:VP1118; -.
DR PATRIC; fig|223926.6.peg.1060; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_042266_1_0_6; -.
DR OMA; AVCCTEG; -.
DR EvolutionaryTrace; Q87QN1; -.
DR Proteomes; UP000002493; Chromosome 1.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..287
FT /note="Protease HtpX"
FT /id="PRO_0000138904"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 36..56
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 192..212
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT ACT_SITE 144
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 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:3CQB"
FT HELIX 77..93
FT /evidence="ECO:0007829|PDB:3CQB"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3CQB"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:3CQB"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:3CQB"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:3CQB"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:3CQB"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:3CQB"
SQ SEQUENCE 287 AA; 31082 MW; D35DB10325654182 CRC64;
MKRIMLFLAT NLAVVLVLSV VLNIVYATTG MQPGSLSGLL VMAAVFGFGG ALISLMMSKG
MALRSVGGMV IESPRNETEH WLLETVGRQA QQAGIGMPTV AIYDSADINA FATGAKRDDS
LVAVSTGLLH NMTRDEAEAV LAHEVSHIAN GDMVTMTLMQ GVVNTFVIFL SRFIANIVAS
NDDEEGQGTN MMVYFGVSMV LELVFGFLAS FITMWYSRHR EFHADAGAAR LVGKEKMIAA
LERLKMSQES KLDGTMMAFG INGKQSLTEL LMSHPPLDKR IAALRNQ
