(data stored in ACNUC7421 zone)

SWISSPROT: HTPX_LEGPC

ID   HTPX_LEGPC              Reviewed;         280 AA.
AC   A5IA60;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 74.
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=LPC_0264;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP000675; ABQ54260.1; -; Genomic_DNA.
DR   RefSeq; WP_011945434.1; NC_009494.2.
DR   EnsemblBacteria; ABQ54260; ABQ54260; LPC_0264.
DR   KEGG; lpc:LPC_0264; -.
DR   HOGENOM; HOG000227301; -.
DR   KO; K03799; -.
DR   OMA; AVCCTEG; -.
DR   BioCyc; LPNE400673:LPC_RS01245-MONOMER; -.
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   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.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5IA60.
DR   SWISS-2DPAGE; A5IA60.
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Stress response; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..280
FT                   /note="Protease HtpX"
FT                   /id="PRO_1000077467"
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        30..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   METAL           129
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   METAL           133
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   METAL           203
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   280 AA;  30293 MW;  4130930E8AF4A559 CRC64;
     MINNLKTFIL LASLTALLVV IGGLLGGSTG MLVALLFAGI MNFSAYWYSD TLVLKMYNAE
     PLSNNHFVYH IVSELAHRAG TSVPKVYLIN NSTPNAFATG RNPENASIAV TTGLLDRLTQ
     EEITGVLAHE LAHVIHRDTL INVVSATIAG AISGIANMFM WLSMFGHNSN NEEGVHPVVG
     MIMMIVAPLA AGLIQMAISR SREFEADAGG ARISGNPQWL ASALLKLDQA NHEQYFDEAE
     THPATAHLFI INPLNGEKLA NLFSTHPSTA ERVARLRAMY
//

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