YVCJ_BACSU
ID YVCJ_BACSU Reviewed; 295 AA.
AC O06973;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Nucleotide-binding protein YvcJ {ECO:0000255|HAMAP-Rule:MF_00636};
GN Name=yvcJ; OrderedLocusNames=BSU34770;
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;
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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, NTPASE ACTIVITY, KINETIC PARAMETERS, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=19074378; DOI=10.1128/jb.01493-08;
RA Luciano J., Foulquier E., Fantino J.R., Galinier A., Pompeo F.;
RT "Characterization of YvcJ, a conserved P-loop-containing protein, and its
RT implication in competence in Bacillus subtilis.";
RL J. Bacteriol. 191:1556-1564(2009).
CC -!- FUNCTION: Displays ATPase and GTPase activities. Can also hydrolyze
CC pNPP. May affect the expression of competence via the phosphorylation
CC of a cellular component. {ECO:0000269|PubMed:19074378}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=GTP is hydrolyzed with a 2-fold higher efficiency than ATP.
CC {ECO:0000269|PubMed:19074378};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a reduction in
CC transformation efficiency and in fraction of cells that express
CC competence. {ECO:0000269|PubMed:19074378}.
CC -!- SIMILARITY: Belongs to the RapZ-like family. {ECO:0000255|HAMAP-
CC Rule:MF_00636}.
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DR EMBL; Z94043; CAB08057.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15482.1; -; Genomic_DNA.
DR PIR; H70031; H70031.
DR RefSeq; NP_391357.1; NC_000964.3.
DR RefSeq; WP_003243903.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O06973; -.
DR SMR; O06973; -.
DR IntAct; O06973; 2.
DR STRING; 224308.BSU34770; -.
DR jPOST; O06973; -.
DR PaxDb; O06973; -.
DR PRIDE; O06973; -.
DR EnsemblBacteria; CAB15482; CAB15482; BSU_34770.
DR GeneID; 936532; -.
DR KEGG; bsu:BSU34770; -.
DR PATRIC; fig|224308.179.peg.3765; -.
DR eggNOG; COG1660; Bacteria.
DR InParanoid; O06973; -.
DR OMA; TVMSFGF; -.
DR PhylomeDB; O06973; -.
DR BioCyc; BSUB:BSU34770-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00636; RapZ_like; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005337; RapZ-like.
DR PANTHER; PTHR30448; PTHR30448; 1.
DR Pfam; PF03668; ATP_bind_2; 1.
DR PIRSF; PIRSF005052; P-loopkin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..295
FT /note="Nucleotide-binding protein YvcJ"
FT /id="PRO_0000107689"
FT BINDING 16..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
FT BINDING 67..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
SQ SEQUENCE 295 AA; 33851 MW; 4D717DCB4459F92A CRC64;
MSVSESHDIQ LVIITGMSGA GKTVAIQSFE DLGYFCVDNL PPSLLPKFLE LMKESNSKMS
KVALVMDLRG REFFDRLIEA LDEMAENPWI TPRILFLDAK DSILVTRYKE TRRSHPLAAT
GLPLEGIALE RELLEELKGR SQIIYDTSDM KPRDLREKIV KHFATNQGET FTVNVMSFGF
KYGIPIDADL VFDVRFLPNP YYIESMRPLT GKDKEVSSYV MKWNETQKFN EKLIDLLSFM
LPSYKREGKS QVVIAIGCTG GQHRSVTLAE NLADYFKKDY YTHVTHRDIE KRSRK
