HTPX_BACFN
ID HTPX_BACFN Reviewed; 322 AA.
AC Q5LE03;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=BF1952;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(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}.
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DR EMBL; CR626927; CAH07650.1; -; Genomic_DNA.
DR RefSeq; WP_005800413.1; NC_003228.3.
DR AlphaFoldDB; Q5LE03; -.
DR STRING; 272559.BF9343_1869; -.
DR EnsemblBacteria; CAH07650; CAH07650; BF9343_1869.
DR GeneID; 66329284; -.
DR KEGG; bfs:BF9343_1869; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_042266_2_0_10; -.
DR OMA; AVCCTEG; -.
DR OrthoDB; 1918093at2; -.
DR Proteomes; UP000006731; 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; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..322
FT /note="Protease HtpX homolog"
FT /id="PRO_1000192737"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT ACT_SITE 166
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ SEQUENCE 322 AA; 36115 MW; C17B57E70CD2B519 CRC64;
MQYVGIQTQQ SRNNLRSGIL LILFPCLVAV LTYLFCYLLI TFTVEDDYGQ YNTLAMTNQM
FINLIPYIIG GVLVWFIIAY FTNSSIIKAA TGARPLERKE NKRIYNLVEN LCMSQGMKMP
KINIIDDDSL NAYASGINEQ TYTVTLSKGI IEKLNDEELE GVIAHELTHI RNHDVRLLII
SIVFVGIFSM LAQIALRSVY YSSWTRSRND KNNGAILILV LAMIVAAIGY FFATLMRFAI
SRKREYMADA GAAEMTKNPL ALASALRKIS ADPDIEAVER EDVAQLFIQH PGKQAKSALS
GLSGLFATHP PIEKRIAILE QF