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MECA_STRMU
ID   MECA_STRMU              Reviewed;         240 AA.
AC   Q8DW33; Q9XDW9;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Adapter protein MecA {ECO:0000255|HAMAP-Rule:MF_01124};
GN   Name=mecA {ECO:0000255|HAMAP-Rule:MF_01124}; OrderedLocusNames=SMU_245;
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=Xc / Serotype c;
RX   PubMed=10515952; DOI=10.1128/jb.181.20.6556-6559.1999;
RA   Yamashita Y., Shibata Y., Nakano Y., Tsuda H., Kido N., Ohta M., Koga T.;
RT   "A novel gene required for rhamnose-glucose polysaccharide synthesis in
RT   Streptococcus mutans.";
RL   J. Bacteriol. 181:6556-6559(1999).
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   -!- FUNCTION: Enables the recognition and targeting of unfolded and
CC       aggregated proteins to the ClpC protease or to other proteins involved
CC       in proteolysis. {ECO:0000255|HAMAP-Rule:MF_01124}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01124}.
CC   -!- DOMAIN: The N-terminal domain probably binds unfolded/aggregated
CC       proteins; the C-terminal domain interacts with ClpC.
CC   -!- SIMILARITY: Belongs to the MecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01124}.
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DR   EMBL; AB022909; BAA82113.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN58015.1; -; Genomic_DNA.
DR   RefSeq; NP_720709.1; NC_004350.2.
DR   RefSeq; WP_002262749.1; NC_004350.2.
DR   AlphaFoldDB; Q8DW33; -.
DR   SMR; Q8DW33; -.
DR   STRING; 210007.SMU_245; -.
DR   PRIDE; Q8DW33; -.
DR   EnsemblBacteria; AAN58015; AAN58015; SMU_245.
DR   KEGG; smu:SMU_245; -.
DR   PATRIC; fig|210007.7.peg.212; -.
DR   eggNOG; COG4862; Bacteria.
DR   HOGENOM; CLU_071496_1_0_9; -.
DR   OMA; EFFYTVM; -.
DR   PhylomeDB; Q8DW33; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.1950; -; 1.
DR   HAMAP; MF_01124; MecA; 1.
DR   InterPro; IPR038471; MecA_C_sf.
DR   InterPro; IPR008681; Neg-reg_MecA.
DR   PANTHER; PTHR39161; PTHR39161; 1.
DR   Pfam; PF05389; MecA; 1.
DR   PIRSF; PIRSF029008; MecA; 1.
PE   3: Inferred from homology;
KW   Reference proteome.
FT   CHAIN           1..240
FT                   /note="Adapter protein MecA"
FT                   /id="PRO_0000212288"
FT   CONFLICT        56
FT                   /note="D -> G (in Ref. 1; BAA82113)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="N -> S (in Ref. 1; BAA82113)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   240 AA;  28056 MW;  96DA18BBCB865FC5 CRC64;
     MEMKQISETT LKITISMEDL EERGMELKDF LIPQEKTEEF FYTVMDELDL PENFKDSGML
     SFRVTPRNDR IDVFVTKSEI NKNLNLEDLS DFDDISKMSP EDFFNTLEET MREKGDAAAL
     DKLAEIEKRE EEKTQQEKGE TKEKRDYVHF VLDFPNIQQV INFAKTVDYD VEASELFKES
     DAYHMTVLLN LEDKPDYYAD LMFARMLEHA GRGTKTRAYL LEHGVQLIKA DALQELQMIG
 
 
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