CSSR_BACSU
ID CSSR_BACSU Reviewed; 225 AA.
AC O32192; O32304;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Transcriptional regulatory protein CssR;
GN Name=cssR; OrderedLocusNames=BSU33010;
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 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 [5]
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.
CC {ECO:0000269|PubMed:11717295}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by CssS. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB07967.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z93941; CAB07967.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AJ223978; CAA11752.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15291.1; -; Genomic_DNA.
DR PIR; C70045; C70045.
DR RefSeq; NP_391181.1; NC_000964.3.
DR RefSeq; WP_003228529.1; NZ_JNCM01000033.1.
DR PDB; 7CX5; X-ray; 1.07 A; A=133-225.
DR PDBsum; 7CX5; -.
DR AlphaFoldDB; O32192; -.
DR SMR; O32192; -.
DR STRING; 224308.BSU33010; -.
DR PaxDb; O32192; -.
DR PRIDE; O32192; -.
DR EnsemblBacteria; CAB15291; CAB15291; BSU_33010.
DR GeneID; 938594; -.
DR KEGG; bsu:BSU33010; -.
DR PATRIC; fig|224308.179.peg.3577; -.
DR eggNOG; COG0745; Bacteria.
DR InParanoid; O32192; -.
DR OMA; EMGSDDY; -.
DR PhylomeDB; O32192; -.
DR BioCyc; BSUB:BSU33010-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..225
FT /note="Transcriptional regulatory protein CssR"
FT /id="PRO_0000081083"
FT DOMAIN 4..117
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 129..224
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 52
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:7CX5"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:7CX5"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:7CX5"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:7CX5"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:7CX5"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:7CX5"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:7CX5"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:7CX5"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:7CX5"
SQ SEQUENCE 225 AA; 26212 MW; EF4105B7FCDBEFD2 CRC64;
MSYTIYLVED EDNLNELLTK YLENEGWNIT SFTKGEDARK KMTPSPHLWI LDIMLPDTDG
YTLIKEIKAK DPDVPVIFIS ARDADIDRVL GLELGSNDYI SKPFLPRELI IRVQKLLQLV
YKEAPPVQKN EIAVSSYRVA EDAREVYDEN GNIINLTSKE FDLLLLFIHH KGHPYSREDI
LLKVWGHDYF GTDRVVDDLV RRLRRKMPEL KVETIYGFGY RMMSS
