(data stored in ACNUC7421 zone)

SWISSPROT: D6XXB2_BACIE

ID   D6XXB2_BACIE            Unreviewed;       304 AA.
AC   D6XXB2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=Protease HtpX homolog {ECO:0000256|HAMAP-Rule:MF_00188};
DE            EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_00188};
GN   Name=htpX {ECO:0000256|HAMAP-Rule:MF_00188};
GN   OrderedLocusNames=Bsel_0431 {ECO:0000313|EMBL:ADH97969.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97969.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97969.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00188};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00188};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00188}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00188}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family.
CC       {ECO:0000256|HAMAP-Rule:MF_00188, ECO:0000256|SAAS:SAAS00541274}.
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DR   EMBL; CP001791; ADH97969.1; -; Genomic_DNA.
DR   RefSeq; WP_013171398.1; NC_014219.1.
DR   STRING; 439292.Bsel_0431; -.
DR   MEROPS; M48.002; -.
DR   EnsemblBacteria; ADH97969; ADH97969; Bsel_0431.
DR   KEGG; bse:Bsel_0431; -.
DR   eggNOG; COG0501; LUCA.
DR   HOGENOM; HOG000227302; -.
DR   KO; K03799; -.
DR   OMA; REYMADS; -.
DR   OrthoDB; 1918093at2; -.
DR   BioCyc; BSEL439292:G1GLR-462-MONOMER; -.
DR   Proteomes; UP000000271; 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   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;
DR   PRODOM; D6XXB2.
DR   SWISS-2DPAGE; D6XXB2.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00423899};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00112036};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00016464};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00473692};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00112271};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00473645};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00016455};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00016434};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00188, ECO:0000256|SAAS:SAAS00473636}.
FT   TRANSMEM      7     27       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
FT   TRANSMEM     47     68       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
FT   TRANSMEM    176    196       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
FT   TRANSMEM    202    227       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
FT   DOMAIN       90    302       Peptidase_M48. {ECO:0000259|Pfam:
FT                                PF01435}.
FT   ACT_SITE    158    158       {ECO:0000256|HAMAP-Rule:MF_00188}.
FT   METAL       157    157       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
FT   METAL       161    161       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
FT   METAL       232    232       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
SQ   SEQUENCE   304 AA;  33421 MW;  2B8ABDA584451374 CRC64;
     MGKRFFFFLL TNIMVMVTIL IVWSLITEFT DLGRTFDTGG PGLGIDLVSL AVFSILIGFM
     GSFISLAMSR FVAKKMMKVK VIDPDGPMSQ EERIVVEKVH RLSRAAGLMH MPEVGIYQSQ
     EVNAFATGPS KKKSLVAVSS GLLHVMDDDA VEGVIAHEVA HVANGDMVTM TLLQGVINTF
     VVFFSRIIAI VASRLVPEQY QFIVQLASII IFQILLSILG SIVVMAYSRY REFHADRGGA
     DLAGKDKMAH ALRSLQSYVD RASVNRGRDD SAVQTMKISG KRGMSLMFSS HPDLGERIAR
     LEGK
//

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