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YYCI_BACSU
ID   YYCI_BACSU              Reviewed;         280 AA.
AC   Q45612; Q794W1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Two-component system WalR/WalK regulatory protein YycI;
GN   Name=yycI; OrderedLocusNames=BSU40380;
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=9205843; DOI=10.1093/dnares/4.2.155;
RA   Kasahara Y., Nakai S., Ogasawara N.;
RT   "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT   Bacillus subtilis genome.";
RL   DNA Res. 4:155-159(1997).
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, TOPOLOGY, DISRUPTION PHENOTYPE, AND INTERACTION WITH WALK AND
RP   YYCH.
RX   PubMed=17307850; DOI=10.1128/jb.01936-06;
RA   Szurmant H., Mohan M.A., Imus P.M., Hoch J.A.;
RT   "YycH and YycI interact to regulate the essential YycFG two-component
RT   system in Bacillus subtilis.";
RL   J. Bacteriol. 189:3280-3289(2007).
RN   [4]
RP   FUNCTION, MUTAGENESIS OF PHE-10; PHE-14; ASP-18; LEU-21 AND PHE-25, AND
RP   DOMAIN.
RX   PubMed=18408157; DOI=10.1073/pnas.0800247105;
RA   Szurmant H., Bu L., Brooks C.L. III, Hoch J.A.;
RT   "An essential sensor histidine kinase controlled by transmembrane helix
RT   interactions with its auxiliary proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5891-5896(2008).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 31-280, AND SUBUNIT.
RX   PubMed=17307848; DOI=10.1128/jb.01937-06;
RA   Santelli E., Liddington R.C., Mohan M.A., Hoch J.A., Szurmant H.;
RT   "The crystal structure of Bacillus subtilis YycI reveals a common fold for
RT   two members of an unusual class of sensor histidine kinase regulatory
RT   proteins.";
RL   J. Bacteriol. 189:3290-3295(2007).
CC   -!- FUNCTION: Together with YycH, regulates the activity of the two-
CC       component system WalR/WalK. {ECO:0000269|PubMed:17307850,
CC       ECO:0000269|PubMed:18408157}.
CC   -!- SUBUNIT: Homodimer. Interacts with WalK and YycH.
CC       {ECO:0000269|PubMed:17307848, ECO:0000269|PubMed:17307850}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The transmembrane region is required for the regulation of WalK
CC       activity. {ECO:0000269|PubMed:18408157}.
CC   -!- DISRUPTION PHENOTYPE: Induction of WalR-dependent gene expression. Cell
CC       wall defect. {ECO:0000269|PubMed:17307850}.
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DR   EMBL; D78193; BAA11297.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB16075.1; -; Genomic_DNA.
DR   PIR; H70089; H70089.
DR   RefSeq; NP_391918.1; NC_000964.3.
DR   RefSeq; WP_003244037.1; NZ_JNCM01000034.1.
DR   PDB; 2O3O; X-ray; 2.89 A; A/B/C/D/E/F/G/H/I/J/K/L=31-280.
DR   PDBsum; 2O3O; -.
DR   AlphaFoldDB; Q45612; -.
DR   SMR; Q45612; -.
DR   STRING; 224308.BSU40380; -.
DR   PaxDb; Q45612; -.
DR   PRIDE; Q45612; -.
DR   EnsemblBacteria; CAB16075; CAB16075; BSU_40380.
DR   GeneID; 937765; -.
DR   KEGG; bsu:BSU40380; -.
DR   PATRIC; fig|224308.179.peg.4371; -.
DR   eggNOG; COG4853; Bacteria.
DR   OMA; TWHIVVN; -.
DR   PhylomeDB; Q45612; -.
DR   BioCyc; BSUB:BSU40380-MON; -.
DR   EvolutionaryTrace; Q45612; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR018604; YycI-like.
DR   Pfam; PF09648; YycI; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..280
FT                   /note="Two-component system WalR/WalK regulatory protein
FT                   YycI"
FT                   /id="PRO_0000360822"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..280
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         10
FT                   /note="F->A: Induction of WalK-dependent genes."
FT                   /evidence="ECO:0000269|PubMed:18408157"
FT   MUTAGEN         14
FT                   /note="F->A: Induction of WalK-dependent genes."
FT                   /evidence="ECO:0000269|PubMed:18408157"
FT   MUTAGEN         18
FT                   /note="D->A: Induction of WalK-dependent genes."
FT                   /evidence="ECO:0000269|PubMed:18408157"
FT   MUTAGEN         21
FT                   /note="L->A: Induction of WalK-dependent genes."
FT                   /evidence="ECO:0000269|PubMed:18408157"
FT   MUTAGEN         25
FT                   /note="F->A: Induction of WalK-dependent genes."
FT                   /evidence="ECO:0000269|PubMed:18408157"
FT   HELIX           35..49
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          62..71
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   HELIX           76..79
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          99..110
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   HELIX           116..127
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          134..140
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   TURN            141..144
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          145..152
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   HELIX           164..166
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          168..175
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          177..187
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          189..200
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   HELIX           203..212
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          221..235
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          238..252
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          261..269
FT                   /evidence="ECO:0007829|PDB:2O3O"
FT   STRAND          274..277
FT                   /evidence="ECO:0007829|PDB:2O3O"
SQ   SEQUENCE   280 AA;  32594 MW;  991C958F77F58C77 CRC64;
     MEWNKTKSIF IVAFLILDIF LGYQFFQKWQ ATGKEYEVIK NDVEHDMKAD HITYEGLNKE
     ATEGYRITAN QKSFSKEEIE ALKDQKPLMD MPSDDHKVTS LKMKFANPIA LSKKDIEDDA
     QALVSSKIQD GEKYKLWKVD KSKKEIIFFQ TYEGHYIYQK TDNPSNMIGQ VVLHLNGKNE
     VVSYDQTTLE TFKQIQKESL ITEMDAVELL YYQNQLKEYS TVKSCKFGYV AQYPLTSTQV
     LAPVWRITVE YEKKVNGEKK TVQEYFTVNA LESTILDTDQ
 
 
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