ID   HTPX_STRMU              Reviewed;         299 AA.
AC   Q93D93;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=SMU_1929;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT11;
RA   Tao L., Tanzer J.M.;
RT   "Novel sucrose-dependent adhesion cofactors (sdc) in Streptococcus
RT   mutans.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AF397166; AAL04088.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59540.1; -; Genomic_DNA.
DR   RefSeq; NP_722234.1; NC_004350.2.
DR   RefSeq; WP_002262126.1; NC_004350.2.
DR   AlphaFoldDB; Q93D93; -.
DR   STRING; 210007.SMU_1929; -.
DR   PRIDE; Q93D93; -.
DR   EnsemblBacteria; AAN59540; AAN59540; SMU_1929.
DR   GeneID; 66818734; -.
DR   KEGG; smu:SMU_1929; -.
DR   PATRIC; fig|210007.7.peg.1715; -.
DR   eggNOG; COG0501; Bacteria.
DR   HOGENOM; CLU_042266_2_1_9; -.
DR   OMA; AVCCTEG; -.
DR   PhylomeDB; Q93D93; -.
DR   Proteomes; UP000002512; 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..299
FT                   /note="Protease HtpX homolog"
FT                   /id="PRO_0000138895"
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        198..218
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         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   299 AA;  32725 MW;  6409CB04766D9F8B CRC64;
     MLFNQIASNK RKTIVLLIVF FMLLAAIGAA VGYLWLDSLV GGMAIALIIG FIYAFSMIFQ
     STNIVMAMNN AKEITVDEMP DYYHIVEDMA MVAQIPMPRV YVIDDPSLNA FATGSSPQNA
     AVAATTGLLA IMNREELEGV IGHEVSHIRN YDIRISTIAV ALASAVTLIS SIGGRMMWFG
     GGRSRRSNDN EGGGYLQIIL LIFSLLAIIL APLAASLVQL AISRQREYLA DASSVELTRN
     PQGMIRALQK LEQSQPMAHS VDNASAALYI NDPKKKSGLK HLFYTHPPIA DRIRRLEQV