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CSSS_BACSU
ID   CSSS_BACSU              Reviewed;         451 AA.
AC   O32193; O32303;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Sensor histidine kinase CssS;
DE            EC=2.7.13.3;
GN   Name=cssS; Synonyms=yvqB; OrderedLocusNames=BSU33020;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9353931; DOI=10.1099/00221287-143-10-3305;
RA   Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT   "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT   degrees) in Bacillus subtilis.";
RL   Microbiology 143:3305-3308(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9639930; DOI=10.1099/00221287-144-6-1593;
RA   Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.;
RT   "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis
RT   chromosome containing genes involved in metal ion uptake and a putative
RT   sigma factor.";
RL   Microbiology 144:1593-1600(1998).
RN   [3]
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   [4]
RP   SEQUENCE REVISION TO 444.
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   [5]
RP   FUNCTION.
RX   PubMed=11717295; DOI=10.1128/jb.183.24.7365-7370.2001;
RA   Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T.,
RA   Fujita Y.;
RT   "Comprehensive DNA microarray analysis of Bacillus subtilis two-component
RT   regulatory systems.";
RL   J. Bacteriol. 183:7365-7370(2001).
RN   [6]
RP   CHARACTERIZATION.
RC   STRAIN=168;
RX   PubMed=11555295; DOI=10.1046/j.1365-2958.2001.02576.x;
RA   Hyyrylaeinen H.-L., Bolhuis A., Darmon E., Muukkonen L., Koski P.,
RA   Vitikainen M., Sarvas M., Pragai Z., Bron S., van Dijl J.M., Kontinen V.P.;
RT   "A novel two-component regulatory system in Bacillus subtilis for the
RT   survival of severe secretion stress.";
RL   Mol. Microbiol. 41:1159-1172(2001).
CC   -!- FUNCTION: Member of the two-component regulatory system CssS/CssR
CC       required to control the cellular response to secretion stress. Required
CC       for the transcription of htrA. Could detect misfolded proteins at the
CC       membrane-cell wall interface and then activate CssR by phosphorylation.
CC       {ECO:0000269|PubMed:11717295}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB07976.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z93941; CAB07976.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AJ223978; CAA11751.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15292.2; -; Genomic_DNA.
DR   PIR; D70045; D70045.
DR   RefSeq; NP_391182.2; NC_000964.3.
DR   RefSeq; WP_003228527.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32193; -.
DR   SMR; O32193; -.
DR   IntAct; O32193; 16.
DR   STRING; 224308.BSU33020; -.
DR   PaxDb; O32193; -.
DR   PRIDE; O32193; -.
DR   EnsemblBacteria; CAB15292; CAB15292; BSU_33020.
DR   GeneID; 935936; -.
DR   KEGG; bsu:BSU33020; -.
DR   PATRIC; fig|224308.179.peg.3578; -.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG2770; Bacteria.
DR   InParanoid; O32193; -.
DR   OMA; IKMWMAS; -.
DR   PhylomeDB; O32193; -.
DR   BioCyc; BSUB:BSU33020-MON; -.
DR   BRENDA; 2.7.13.3; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..451
FT                   /note="Sensor histidine kinase CssS"
FT                   /id="PRO_0000074743"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..165
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..451
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          187..239
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          247..451
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         250
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   CONFLICT        444
FT                   /note="T -> S (in Ref. 2; CAA11751)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   451 AA;  52097 MW;  DCC269B9038176F0 CRC64;
     MKNKPLAFQI WVVISGILLA ISILLLVLFS NTLRDFFTNE TYTTIENEQH VLTEYRLPGS
     IERRYYSEEA TAPTTVRSVQ HVLLPENEEA SSDKDLSILS SSFIHKVYKL ADKQEAKKKR
     YSADVNGEKV FFVIKKGLSV NGQSAMMLSY ALDSYRDDLA YTLFKQLLFI IAVVILLSWI
     PAIWLAKYLS RPLVSFEKHV KRISEQDWDD PVKVDRKDEI GKLGHTIEEM RQKLVQKDET
     ERTLLQNISH DLKTPVMVIR GYTQSIKDGI FPKGDLENTV DVIECEALKL EKKIKDLLYL
     TKLDYLAKQK VQHDMFSIVE VTEEVIERLK WARKELSWEI DVEEDILMPG DPEQWNKLLE
     NILENQIRYA ETKIEISMKQ DDRNIVITIK NDGPHIEDEM LSSLYEPFNK GKKGEFGIGL
     SIVKRILTLH KASISIENDK TGVTYRIAVP K
 
 
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