CSPD_ECOLI
ID CSPD_ECOLI Reviewed; 74 AA.
AC P0A968; P24245;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cold shock-like protein CspD;
DE Short=CSP-D;
GN Name=cspD; Synonyms=cspH, ybjA; OrderedLocusNames=b0880, JW0864;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2186030; DOI=10.1016/s0021-9258(19)39014-3;
RA Gottesman S., Clark W.P., Maurizi M.R.;
RT "The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and
RT identification of a Clp-specific substrate.";
RL J. Biol. Chem. 265:7886-7893(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-20.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [6]
RP SIMILARITY TO OTHER CSD PROTEINS.
RX PubMed=1622933;
RA Doniger J., Landsman D., Gonda M.A., Wistow G.;
RT "The product of unr, the highly conserved gene upstream of N-ras, contains
RT multiple repeats similar to the cold-shock domain (CSD), a putative DNA-
RT binding motif.";
RL New Biol. 4:389-395(1992).
RN [7]
RP CHARACTERIZATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=11260474; DOI=10.1046/j.1365-2958.2001.02345.x;
RA Yamanaka K., Zheng W., Crooke E., Wang Y.-H., Inouye M.;
RT "CspD, a novel DNA replication inhibitor induced during the stationary
RT phase in Escherichia coli.";
RL Mol. Microbiol. 39:1572-1584(2001).
RN [8]
RP FUNCTION IN PERSISTER CELL FORMATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=19909729; DOI=10.1016/j.bbrc.2009.11.033;
RA Kim Y., Wood T.K.;
RT "Toxins Hha and CspD and small RNA regulator Hfq are involved in persister
RT cell formation through MqsR in Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 391:209-213(2010).
RN [9]
RP FUNCTION AS A TOXIN, AND INDUCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=20105222; DOI=10.1111/j.1462-2920.2009.02147.x;
RA Kim Y., Wang X., Zhang X.S., Grigoriu S., Page R., Peti W., Wood T.K.;
RT "Escherichia coli toxin/antitoxin pair MqsR/MqsA regulate toxin CspD.";
RL Environ. Microbiol. 12:1105-1121(2010).
CC -!- FUNCTION: Inhibits DNA replication at both initiation and elongation
CC steps, most probably by binding to the opened, single-stranded regions
CC at replication forks. Plays a regulatory role in chromosomal
CC replication in nutrient-depleted cells.
CC -!- FUNCTION: Involved in persister cell formation, acting downstream of
CC mRNA interferase (toxin) MqsR. Overproduction is toxic.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P0A968; P0AAG0: dppD; NbExp=3; IntAct=EBI-547937, EBI-548206;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Not induced by cold-shock. Stationary-phase and starvation
CC inducible, as well as by oxidative stress (30 mM H(2)O(2)). Repressed
CC by MqsA and MqsRA toxin-antitoxin system.
CC {ECO:0000269|PubMed:20105222}.
CC -!- DISRUPTION PHENOTYPE: Deletion represses the production of persister
CC cells. {ECO:0000269|PubMed:19909729}.
CC -!- MISCELLANEOUS: Binds single-stranded DNA and RNA, but not double-
CC stranded DNA, through hydrophobic interactions without sequence
CC specificity, resulting in a packed structure.
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DR EMBL; M31045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAC73967.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35599.1; -; Genomic_DNA.
DR PIR; H64826; H64826.
DR RefSeq; NP_415401.1; NC_000913.3.
DR RefSeq; WP_000410785.1; NZ_STEB01000006.1.
DR AlphaFoldDB; P0A968; -.
DR SMR; P0A968; -.
DR BioGRID; 4263137; 624.
DR BioGRID; 850041; 1.
DR DIP; DIP-47833N; -.
DR IntAct; P0A968; 39.
DR STRING; 511145.b0880; -.
DR jPOST; P0A968; -.
DR PaxDb; P0A968; -.
DR PRIDE; P0A968; -.
DR EnsemblBacteria; AAC73967; AAC73967; b0880.
DR EnsemblBacteria; BAA35599; BAA35599; BAA35599.
DR GeneID; 67414639; -.
DR GeneID; 945669; -.
DR KEGG; ecj:JW0864; -.
DR KEGG; eco:b0880; -.
DR PATRIC; fig|1411691.4.peg.1397; -.
DR EchoBASE; EB1102; -.
DR eggNOG; COG1278; Bacteria.
DR HOGENOM; CLU_117621_0_2_6; -.
DR InParanoid; P0A968; -.
DR OMA; HYSTIKM; -.
DR PhylomeDB; P0A968; -.
DR BioCyc; EcoCyc:EG11111-MON; -.
DR PRO; PR:P0A968; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003676; F:nucleic acid binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:EcoCyc.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:EcoCyc.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008156; P:negative regulation of DNA replication; IDA:EcoCyc.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0042594; P:response to starvation; IDA:EcoliWiki.
DR CDD; cd04458; CSP_CDS; 1.
DR DisProt; DP02900; -.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012156; Cold_shock_CspA.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR019844; CSD_1.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012751; CspD.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF00313; CSD; 1.
DR PIRSF; PIRSF002599; Cold_shock_A; 1.
DR PRINTS; PR00050; COLDSHOCK.
DR SMART; SM00357; CSP; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR02381; cspD; 1.
DR PROSITE; PS00352; CSD_1; 1.
DR PROSITE; PS51857; CSD_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; DNA replication inhibitor;
KW DNA-binding; Reference proteome; RNA-binding; Toxin.
FT CHAIN 1..74
FT /note="Cold shock-like protein CspD"
FT /id="PRO_0000100248"
FT DOMAIN 4..64
FT /note="CSD"
FT CONFLICT 19
FT /note="C -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 74 AA; 7969 MW; C74AB028135BC22C CRC64;
MEKGTVKWFN NAKGFGFICP EGGGEDIFAH YSTIQMDGYR TLKAGQSVQF DVHQGPKGNH
ASVIVPVEVE AAVA
