HTPX_STRSV
ID HTPX_STRSV Reviewed; 298 AA.
AC A3CLJ7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=SSA_0611;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00188};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00188}.
CC -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000255|HAMAP-
CC Rule:MF_00188}.
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DR EMBL; CP000387; ABN44052.1; -; Genomic_DNA.
DR RefSeq; WP_011836621.1; NC_009009.1.
DR RefSeq; YP_001034602.1; NC_009009.1.
DR AlphaFoldDB; A3CLJ7; -.
DR SMR; A3CLJ7; -.
DR STRING; 388919.SSA_0611; -.
DR EnsemblBacteria; ABN44052; ABN44052; SSA_0611.
DR KEGG; ssa:SSA_0611; -.
DR PATRIC; fig|388919.9.peg.589; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_042266_2_1_9; -.
DR OMA; AVCCTEG; -.
DR OrthoDB; 1918093at2; -.
DR Proteomes; UP000002148; 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 membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..298
FT /note="Protease HtpX homolog"
FT /id="PRO_1000020956"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT ACT_SITE 144
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 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ SEQUENCE 298 AA; 32518 MW; 3696820020BD05B2 CRC64;
MLFDQIASNK RRTWLLLIAF FGLLALLGAA IGYLWLRSAV GGVLLALIIG AIYAGVMIFQ
STEVVMAMNG AREVSEQEAP ELYHIVQDMA MVAQIPMPRV YIVEDPSPNA FATGSKPENA
AVAATTGILQ IMNREELEGV IGHEVSHIRN YDIRISTIAV ALASAITMLS SLAGRMMWFG
GGRRSSNDRD NDSGLGIILL IVSLIAIVLA PLAATLVQLA ISRQREFLAD ASSVELTRNP
QGMINALLKL DRSEPMEHHV DDASAALYIS DPKKEGGLKK LFYTHPPISE RVERLRHM