HTPX_GLAP5
ID HTPX_GLAP5 Reviewed; 283 AA.
AC B8F543;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=HAPS_0810;
OS Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Glaesserella.
OX NCBI_TaxID=557723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH0165;
RX PubMed=19074396; DOI=10.1128/jb.01682-08;
RA Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA Jin M., Jin Q., Chen H.;
RT "Complete genome sequence of Haemophilus parasuis SH0165.";
RL J. Bacteriol. 191:1359-1360(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; CP001321; ACL32445.1; -; Genomic_DNA.
DR RefSeq; WP_005714149.1; NC_011852.1.
DR AlphaFoldDB; B8F543; -.
DR SMR; B8F543; -.
DR STRING; 557723.HAPS_0810; -.
DR MEROPS; M48.002; -.
DR EnsemblBacteria; ACL32445; ACL32445; HAPS_0810.
DR GeneID; 66619107; -.
DR KEGG; hap:HAPS_0810; -.
DR HOGENOM; CLU_042266_1_0_6; -.
DR OMA; AVCCTEG; -.
DR Proteomes; UP000006743; 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..283
FT /note="Protease HtpX"
FT /id="PRO_1000124230"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 147..167
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 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 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ SEQUENCE 283 AA; 30650 MW; 772FC45372334F41 CRC64;
MMRIALFLAT NFAVMIVLGI ILSVTGIAGN STGGILIMSV LFGFAGSLIS LFMSKTMALK
SVGAEIITEP RNNAERWLVE TVKRQSQQAG IPMPDVAIYH SADVNAFATG ATKSNSLVAV
STGLLNTMTE DEAEAVVAHE VAHIANGDMV TMTLLQGVLN TFVIFLSRMI ATAVSSSRND
DGEETQSSGT YFLVSMVLEI LFGVLATIIA MWFSRYREFR ADAGSAQLVG KEKMIAALQR
LQRVHDPEEL PGSLNAMMIN GKAKEFFMSH PPLEKRIEAL RNL