ID   HTPX_STRGC              Reviewed;         297 AA.
AC   O30795; A8AVK1;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Protease HtpX homolog;
DE            EC=3.4.24.-;
GN   Name=htpX; OrderedLocusNames=SGO_0495;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, OPERON STRUCTURE, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11860552; DOI=10.1046/j.0902-0055.2001.00000.x;
RA   Vickerman M.M., Mather N.M., Minick P.E., Edwards C.A.;
RT   "Initial characterization of the Streptococcus gordonii htpX gene.";
RL   Oral Microbiol. Immunol. 17:22-31(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- INDUCTION: Expression is maximal during the early to mid-log stage of
CC       growth and decreases after. Does not respond to heat shock up to 43
CC       degrees Celsius. Part of the lemA-htpX operon.
CC       {ECO:0000269|PubMed:11860552}.
CC   -!- DISRUPTION PHENOTYPE: No effect on extracellular glucosyltransferase
CC       activity, nor on growth characteristics. Deletion does however alter
CC       cell surface appearance, making cells rougher at 41.5 degrees Celsius.
CC       They are also slightly less adhesive on hydroxyapatite.
CC       {ECO:0000269|PubMed:11860552}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000305}.
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DR   EMBL; AF017421; AAB70525.1; -; Genomic_DNA.
DR   EMBL; CP000725; ABV10968.1; -; Genomic_DNA.
DR   PIR; T48855; T48855.
DR   RefSeq; WP_012000001.1; NC_009785.1.
DR   AlphaFoldDB; O30795; -.
DR   SMR; O30795; -.
DR   STRING; 467705.SGO_0495; -.
DR   PRIDE; O30795; -.
DR   EnsemblBacteria; ABV10968; ABV10968; SGO_0495.
DR   KEGG; sgo:SGO_0495; -.
DR   eggNOG; COG0501; Bacteria.
DR   HOGENOM; CLU_042266_2_1_9; -.
DR   OMA; AVCCTEG; -.
DR   Proteomes; UP000001131; 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   2: Evidence at transcript level;
KW   Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..297
FT                   /note="Protease HtpX homolog"
FT                   /id="PRO_0000138894"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   297 AA;  32788 MW;  15EB459D03496D9D CRC64;
     MLFEQIAANK RRTWFLLVAF FALLALIGAA AGYLWMNSPL GGVIIAFIIG LIYAITMIFQ
     STEVVMSMNG ARQVSEQEAP ELYHIVQDMA MVAQIPMPRV YIVEDDSPNA FATGSNPENA
     AVAATTGLLR LMNREELEGV IGHEVSHIRN YDIRISTIAV ALASAITMIS SVAGRMMWYG
     GGRRRNDRDD DSGLGLLMLV FSLIAIILAP LAATLVQLAI SRQREFLADA SSVELTRNPQ
     GMIRALQKLD NSEPMHRHVD DASAALYISD PKKKGGLQKL FYTHPPISER VERLRKM