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 27-MAR-2024, entry version 89.
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; Bacillota; 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 KEGG; smu:SMU_245; -.
DR PATRIC; fig|210007.7.peg.212; -.
DR eggNOG; COG4862; Bacteria.
DR HOGENOM; CLU_071496_1_0_9; -.
DR OrthoDB; 2360201at2; -.
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; ADAPTER PROTEIN MECA; 1.
DR PANTHER; PTHR39161:SF1; ADAPTER PROTEIN MECA; 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
//
