位置:首页 > 蛋白库 > CCPN_BACSU
CCPN_BACSU
ID   CCPN_BACSU              Reviewed;         212 AA.
AC   O34994;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Transcriptional repressor CcpN;
DE   AltName: Full=Catabolite control protein N;
DE   AltName: Full=Control catabolite protein of gluconeogenesis;
GN   Name=ccpN; Synonyms=yqzB; OrderedLocusNames=BSU25250;
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   FUNCTION IN GLUCONEOGENESIS REGULATION, INDUCTION, DNA-BINDING, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15720552; DOI=10.1111/j.1365-2958.2005.04473.x;
RA   Servant P., Le Coq D., Aymerich S.;
RT   "CcpN (YqzB), a novel regulator for CcpA-independent catabolite repression
RT   of Bacillus subtilis gluconeogenic genes.";
RL   Mol. Microbiol. 55:1435-1451(2005).
CC   -!- FUNCTION: Transcription repressor that binds to the promoter of gapB
CC       and pckA genes, preventing their expression. Acts as a regulator for
CC       catabolite repression of gluconeogenic genes.
CC       {ECO:0000269|PubMed:15720552}.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:15720552}.
CC   -!- DISRUPTION PHENOTYPE: Relieves catabolite repression of gapB and pckA
CC       transcription. Disruption is epistatic over a yqfL deletion.
CC       {ECO:0000269|PubMed:15720552}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL009126; CAB14454.1; -; Genomic_DNA.
DR   PIR; A69969; A69969.
DR   RefSeq; NP_390403.1; NC_000964.3.
DR   RefSeq; WP_003237058.1; NZ_JNCM01000036.1.
DR   PDB; 3FV6; X-ray; 1.95 A; A/B=63-212.
DR   PDB; 3FWR; X-ray; 2.45 A; A/B=63-212.
DR   PDB; 3FWS; X-ray; 2.03 A; A/B=63-212.
DR   PDBsum; 3FV6; -.
DR   PDBsum; 3FWR; -.
DR   PDBsum; 3FWS; -.
DR   AlphaFoldDB; O34994; -.
DR   SMR; O34994; -.
DR   IntAct; O34994; 2.
DR   STRING; 224308.BSU25250; -.
DR   PaxDb; O34994; -.
DR   PRIDE; O34994; -.
DR   EnsemblBacteria; CAB14454; CAB14454; BSU_25250.
DR   GeneID; 937886; -.
DR   KEGG; bsu:BSU25250; -.
DR   PATRIC; fig|224308.179.peg.2744; -.
DR   eggNOG; COG0517; Bacteria.
DR   InParanoid; O34994; -.
DR   OMA; SVIMTRM; -.
DR   PhylomeDB; O34994; -.
DR   BioCyc; BSUB:BSU25250-MON; -.
DR   EvolutionaryTrace; O34994; -.
DR   PRO; PR:O34994; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045013; P:carbon catabolite repression of transcription; IMP:CACAO.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.10.580.10; -; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR013196; HTH_11.
DR   InterPro; IPR016842; UCP026546_HTH-CBS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF08279; HTH_11; 1.
DR   PIRSF; PIRSF026546; UCP026546_CBS_YqzB; 1.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..212
FT                   /note="Transcriptional repressor CcpN"
FT                   /id="PRO_0000360044"
FT   DOMAIN          6..70
FT                   /note="HTH deoR-type"
FT   DOMAIN          83..139
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          148..211
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DNA_BIND        23..42
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   HELIX           69..75
FT                   /evidence="ECO:0007829|PDB:3FV6"
FT   HELIX           80..82
FT                   /evidence="ECO:0007829|PDB:3FV6"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:3FV6"
FT   HELIX           96..106
FT                   /evidence="ECO:0007829|PDB:3FV6"
FT   STRAND          109..114
FT                   /evidence="ECO:0007829|PDB:3FV6"
FT   STRAND          120..125
FT                   /evidence="ECO:0007829|PDB:3FV6"
FT   HELIX           126..133
FT                   /evidence="ECO:0007829|PDB:3FV6"
FT   TURN            139..141
FT                   /evidence="ECO:0007829|PDB:3FV6"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:3FV6"
FT   STRAND          148..150
FT                   /evidence="ECO:0007829|PDB:3FV6"
FT   HELIX           163..173
FT                   /evidence="ECO:0007829|PDB:3FV6"
FT   STRAND          176..183
FT                   /evidence="ECO:0007829|PDB:3FV6"
FT   STRAND          185..195
FT                   /evidence="ECO:0007829|PDB:3FV6"
FT   HELIX           196..207
FT                   /evidence="ECO:0007829|PDB:3FV6"
SQ   SEQUENCE   212 AA;  23870 MW;  E001269F2BB93F9E CRC64;
     MSTIELNKRQ EHILQIVKEN GPITGEHIAE KLNLTRATLR PDLAILTMSG FLEARPRVGY
     FYTGKTGTQL LADKLKKLQV KDFQSIPVVI HENVSVYDAI CTMFLEDVGT LFVVDRDAVL
     VGVLSRKDLL RASIGQQELT SVPVHIIMTR MPNITVCRRE DYVMDIAKHL IEKQIDALPV
     IKDTDKGFEV IGRVTKTNMT KILVSLSENE IL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024