MECA2_BACSU
ID MECA2_BACSU Reviewed; 194 AA.
AC P50734;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Adapter protein MecA 2;
GN Name=mecB; Synonyms=ypbH; OrderedLocusNames=BSU22970;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(1996).
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 FUNCTION.
RX PubMed=11914365; DOI=10.1128/jb.184.8.2310-2313.2002;
RA Persuh M., Mandic-Mulec I., Dubnau D.;
RT "A MecA paralog, YpbH, binds ClpC, affecting both competence and
RT sporulation.";
RL J. Bacteriol. 184:2310-2313(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. Also involved in Spx degradation by ClpC (By
CC similarity). Acts negatively in the development of competence by
CC binding ComK and recruiting it to the ClpCP protease. When
CC overexpressed, inhibits sporulation. {ECO:0000250,
CC ECO:0000269|PubMed:11914365}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- DOMAIN: The N-terminal domain has binding sites for ComK and probably
CC for unfolded/aggregated proteins; the C-terminal domain interacts with
CC ClpC.
CC -!- SIMILARITY: Belongs to the MecA family. {ECO:0000305}.
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DR EMBL; L47648; AAC83952.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14213.1; -; Genomic_DNA.
DR PIR; C69933; C69933.
DR RefSeq; NP_390178.1; NC_000964.3.
DR RefSeq; WP_003230533.1; NZ_JNCM01000036.1.
DR PDB; 3JTN; X-ray; 2.09 A; A/B=104-194.
DR PDB; 3JTO; X-ray; 2.40 A; A/B/C/D/E/F=101-194.
DR PDBsum; 3JTN; -.
DR PDBsum; 3JTO; -.
DR AlphaFoldDB; P50734; -.
DR SMR; P50734; -.
DR STRING; 224308.BSU22970; -.
DR PaxDb; P50734; -.
DR PRIDE; P50734; -.
DR EnsemblBacteria; CAB14213; CAB14213; BSU_22970.
DR GeneID; 938980; -.
DR KEGG; bsu:BSU22970; -.
DR PATRIC; fig|224308.179.peg.2504; -.
DR eggNOG; COG4862; Bacteria.
DR OMA; IEMQVKL; -.
DR PhylomeDB; P50734; -.
DR BioCyc; BSUB:BSU22970-MON; -.
DR EvolutionaryTrace; P50734; -.
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; 2.
DR PIRSF; PIRSF029008; MecA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Competence; Reference proteome; Sporulation.
FT CHAIN 1..194
FT /note="Adapter protein MecA 2"
FT /id="PRO_0000212268"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:3JTN"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:3JTN"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:3JTN"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:3JTN"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:3JTN"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:3JTN"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:3JTN"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:3JTN"
SQ SEQUENCE 194 AA; 22157 MW; B27C6ABE4EA0745C CRC64;
MRLERLNYNK IKIFLTLDDL TDRGLTKEDL WKDSFKVHQL FKDMMNEANT ELGFEANGPI
AVEVYSLQAQ GMVVIVTKNQ DADSEDDEYD DDYIEMQVKL DESADIIYQF HSFEDIIQLS
ESLQRIGITG GTVYHYDGQY FLSLEDLGSH TAEGVVAVLA EYGNPTTLTI YRLQEYGKLI
MDGNAVETIQ THFS
