YJBC_BACSU
ID YJBC_BACSU Reviewed; 192 AA.
AC O31601;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Putative acetyltransferase YjbC;
DE EC=2.3.1.-;
GN Name=yjbC; OrderedLocusNames=BSU11490;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP SEQUENCE REVISION TO 130.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [3]
RP SUBCELLULAR LOCATION, AND INDUCTION BY PHOSPHATE STARVATION.
RC STRAIN=168;
RX PubMed=10913081; DOI=10.1128/jb.182.16.4478-4490.2000;
RA Antelmann H., Scharf C., Hecker M.;
RT "Phosphate starvation-inducible proteins of Bacillus subtilis: proteomics
RT and transcriptional analysis.";
RL J. Bacteriol. 182:4478-4490(2000).
RN [4]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=11544224; DOI=10.1128/jb.183.19.5617-5631.2001;
RA Petersohn A., Brigulla M., Haas S., Hoheisel J.D., Voelker U., Hecker M.;
RT "Global analysis of the general stress response of Bacillus subtilis.";
RL J. Bacteriol. 183:5617-5631(2001).
RN [5]
RP INDUCTION.
RC STRAIN=168 / 1604;
RX PubMed=17434969; DOI=10.1128/jb.00130-07;
RA Jervis A.J., Thackray P.D., Houston C.W., Horsburgh M.J., Moir A.;
RT "SigM-responsive genes of Bacillus subtilis and their promoters.";
RL J. Bacteriol. 189:4534-4538(2007).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10913081}.
CC -!- INDUCTION: By different stresses, such as ethanol, salt, and phosphate
CC starvation, in a partially sigma-B dependent manner. Transcribed under
CC partial control of SigM ECF sigma factor (PubMed:17434969).
CC {ECO:0000269|PubMed:10913081, ECO:0000269|PubMed:11544224,
CC ECO:0000269|PubMed:17434969}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display decreased
CC survival rates during salt stress conditions.
CC {ECO:0000269|PubMed:11544224}.
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DR EMBL; AL009126; CAB13006.2; -; Genomic_DNA.
DR RefSeq; NP_389031.2; NC_000964.3.
DR RefSeq; WP_003244921.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31601; -.
DR SMR; O31601; -.
DR STRING; 224308.BSU11490; -.
DR PaxDb; O31601; -.
DR PRIDE; O31601; -.
DR EnsemblBacteria; CAB13006; CAB13006; BSU_11490.
DR GeneID; 939373; -.
DR KEGG; bsu:BSU11490; -.
DR PATRIC; fig|224308.179.peg.1236; -.
DR eggNOG; COG0456; Bacteria.
DR OMA; FIDYLFV; -.
DR PhylomeDB; O31601; -.
DR BioCyc; BSUB:BSU11490-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF13508; Acetyltransf_7; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..192
FT /note="Putative acetyltransferase YjbC"
FT /id="PRO_0000387463"
FT DOMAIN 1..139
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 192 AA; 23120 MW; 6336E2FA1115181A CRC64;
MNWYEKLSEY FPIEEMKSKA HMEALLKERS DIYHKDEGKH HILMFAEFDS FIFVDYLYVS
KDARGQGLGG KLIAKLKKKN KPILLEVEPV DEDDTDTEKR LRFYQREHFK HAQSIGYRRR
SLATNEVNKM EILYWSPKTE SEEEILEAMK QTYENIHTYK DEKWYGESYE KTDEVLEIID
EEKQKNIFDQ LS
