(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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