ID   CSPD_ECOL6              Reviewed;          74 AA.
AC   P0A969; P24245;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cold shock-like protein CspD;
DE            Short=CSP-D;
GN   Name=cspD; OrderedLocusNames=c1017;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: Binds single-stranded DNA and RNA, but not double-
CC       stranded DNA, through hydrophobic interaction without sequence
CC       specificity, resulting in a packed structure. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN79489.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN79489.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000410785.1; NC_004431.1.
DR   AlphaFoldDB; P0A969; -.
DR   SMR; P0A969; -.
DR   STRING; 199310.c1017; -.
DR   EnsemblBacteria; AAN79489; AAN79489; c1017.
DR   GeneID; 67414639; -.
DR   KEGG; ecc:c1017; -.
DR   eggNOG; COG1278; Bacteria.
DR   HOGENOM; CLU_117621_0_2_6; -.
DR   OMA; HYSTIKM; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008156; P:negative regulation of DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd04458; CSP_CDS; 1.
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   3: Inferred from homology;
KW   Cytoplasm; DNA replication inhibitor; DNA-binding; RNA-binding.
FT   CHAIN           1..74
FT                   /note="Cold shock-like protein CspD"
FT                   /id="PRO_0000100250"
FT   DOMAIN          4..64
FT                   /note="CSD"
SQ   SEQUENCE   74 AA;  7969 MW;  C74AB028135BC22C CRC64;
     MEKGTVKWFN NAKGFGFICP EGGGEDIFAH YSTIQMDGYR TLKAGQSVQF DVHQGPKGNH
     ASVIVPVEVE AAVA