MECA1_BACSU
ID MECA1_BACSU Reviewed; 218 AA.
AC P37958;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Adapter protein MecA 1;
GN Name=mecA; OrderedLocusNames=BSU11520;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8412687; DOI=10.1111/j.1365-2958.1993.tb01697.x;
RA Kong L., Siranosian K.J., Grossman A.D., Dubnau D.;
RT "Sequence and properties of mecA, a negative regulator of genetic
RT competence in Bacillus subtilis.";
RL Mol. Microbiol. 9:365-373(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SUBUNIT, AND DOMAIN STRUCTURE.
RC STRAIN=168;
RX PubMed=10447896; DOI=10.1046/j.1365-2958.1999.01544.x;
RA Persuh M., Turgay K., Mandic-Mulec I., Dubnau D.;
RT "The N- and C-terminal domains of MecA recognize different partners in the
RT competence molecular switch.";
RL Mol. Microbiol. 33:886-894(1999).
RN [4]
RP FUNCTION.
RX PubMed=12598648; DOI=10.1073/pnas.0535717100;
RA Schlothauer T., Mogk A., Dougan D.A., Bukau B., Turgay K.;
RT "MecA, an adaptor protein necessary for ClpC chaperone activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2306-2311(2003).
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. Acts negatively in the development of competence by
CC binding ComK and recruiting it to the ClpCP protease. When
CC overexpressed, inhibits sporulation. Also involved in Spx degradation
CC by ClpC. {ECO:0000269|PubMed:12598648}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10447896}.
CC -!- INTERACTION:
CC P37958; P37571: clpC; NbExp=11; IntAct=EBI-5254676, EBI-7349302;
CC -!- DEVELOPMENTAL STAGE: Expressed throughout growth. There is a slight
CC decline of expression during exponential growth and a slight increase
CC after T0.
CC -!- DOMAIN: The N-terminal domain has binding sites for ComK and ComS and
CC probably for unfolded/aggregated proteins; the C-terminal domain
CC interacts with ClpC. {ECO:0000269|PubMed:10447896}.
CC -!- SIMILARITY: Belongs to the MecA family. {ECO:0000305}.
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DR EMBL; L06059; AAC36956.1; -; Unassigned_DNA.
DR EMBL; AL009126; CAB13009.1; -; Genomic_DNA.
DR PIR; S35289; S35289.
DR RefSeq; NP_389034.1; NC_000964.3.
DR RefSeq; WP_003245194.1; NZ_JNCM01000035.1.
DR PDB; 2Y1R; X-ray; 2.60 A; I/J/K/L/M/N/O/P=121-218.
DR PDB; 3J3R; EM; 9.40 A; 1/2/3/4/5/6=1-218.
DR PDB; 3J3S; EM; 11.00 A; 1/2/3/4/5/6=1-218.
DR PDB; 3J3T; EM; 9.00 A; 1/2/3/4/5/6=1-218.
DR PDB; 3J3U; EM; 10.00 A; 1/2/3/4/5/6=1-218.
DR PDB; 3JTP; X-ray; 2.17 A; A/B/C/D=121-218.
DR PDB; 3PXG; X-ray; 3.65 A; a/b/c/d/e/f=121-218.
DR PDB; 3PXI; X-ray; 6.93 A; a/b/c=108-218.
DR PDBsum; 2Y1R; -.
DR PDBsum; 3J3R; -.
DR PDBsum; 3J3S; -.
DR PDBsum; 3J3T; -.
DR PDBsum; 3J3U; -.
DR PDBsum; 3JTP; -.
DR PDBsum; 3PXG; -.
DR PDBsum; 3PXI; -.
DR AlphaFoldDB; P37958; -.
DR BMRB; P37958; -.
DR SMR; P37958; -.
DR DIP; DIP-43709N; -.
DR IntAct; P37958; 2.
DR MINT; P37958; -.
DR STRING; 224308.BSU11520; -.
DR PaxDb; P37958; -.
DR PRIDE; P37958; -.
DR EnsemblBacteria; CAB13009; CAB13009; BSU_11520.
DR GeneID; 936406; -.
DR KEGG; bsu:BSU11520; -.
DR PATRIC; fig|224308.179.peg.1239; -.
DR eggNOG; COG4862; Bacteria.
DR OMA; EFFYTVM; -.
DR PhylomeDB; P37958; -.
DR BioCyc; BSUB:BSU11520-MON; -.
DR EvolutionaryTrace; P37958; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0045808; P:negative regulation of establishment of competence for transformation; IEA:UniProtKB-UniRule.
DR GO; GO:0042174; P:negative regulation of sporulation resulting in formation of a cellular spore; IEA:UniProtKB-UniRule.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Competence; Reference proteome; Sporulation.
FT CHAIN 1..218
FT /note="Adapter protein MecA 1"
FT /id="PRO_0000212267"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:3JTP"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:3JTP"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:3JTP"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:3JTP"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:3JTP"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:3JTP"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:3JTP"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:3JTP"
SQ SEQUENCE 218 AA; 25764 MW; F6E377D8EA241B7D CRC64;
MEIERINEHT VKFYMSYGDI EDRGFDREEI WYNRERSEEL FWEVMDEVHE EEEFAVEGPL
WIQVQALDKG LEIIVTKAQL SKDGQKLELP IPEDKKQEPA SEDLDALLDD FQKEEQAVNQ
EEKEQKLQFV LRFGDFEDVI SLSKLNVNGS KTTLYSFENR YYLYVDFCNM TDEEVENQLS
ILLEYATESS ISIHRLEEYG KLIISEHALE TIKKHFAS
