CSPA_STAA8
ID CSPA_STAA8 Reviewed; 66 AA.
AC Q2FYN2; Q9L534;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Cold shock protein CspA;
GN Name=cspA; OrderedLocusNames=SAOUHSC_01403;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN COLD STRESS RESPONSE, AND
RP SUSCEPTIBILITY TO ANTIMICROBIAL PEPTIDE.
RX PubMed=12874306; DOI=10.1128/iai.71.8.4304-4312.2003;
RA Katzif S., Danavall D., Bowers S., Balthazar J.T., Shafer W.M.;
RT "The major cold shock gene, cspA, is involved in the susceptibility of
RT Staphylococcus aureus to an antimicrobial peptide of human cathepsin G.";
RL Infect. Immun. 71:4304-4312(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP FUNCTION IN PIGMENT PRODUCTION.
RX PubMed=16291691; DOI=10.1128/jb.187.23.8181-8184.2005;
RA Katzif S., Lee E.-H., Law A.B., Tzeng Y.-L., Shafer W.M.;
RT "CspA regulates pigment production in Staphylococcus aureus through a SigB-
RT dependent mechanism.";
RL J. Bacteriol. 187:8181-8184(2005).
CC -!- FUNCTION: Involved in cold stress response and in the susceptibility to
CC an antimicrobial peptide of human cathepsin G (CG117-136). Regulates
CC yellowish-orange pigment production through a still unclear SigB-
CC dependent mechanism. {ECO:0000269|PubMed:12874306,
CC ECO:0000269|PubMed:16291691}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Up-regulated in response to low temperature.
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DR EMBL; AF259960; AAF72664.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30497.1; -; Genomic_DNA.
DR RefSeq; WP_000809131.1; NZ_LS483365.1.
DR RefSeq; YP_499930.1; NC_007795.1.
DR AlphaFoldDB; Q2FYN2; -.
DR SMR; Q2FYN2; -.
DR STRING; 1280.SAXN108_1419; -.
DR EnsemblBacteria; ABD30497; ABD30497; SAOUHSC_01403.
DR GeneID; 3920693; -.
DR GeneID; 66839594; -.
DR KEGG; sao:SAOUHSC_01403; -.
DR PATRIC; fig|93061.5.peg.1284; -.
DR eggNOG; COG1278; Bacteria.
DR HOGENOM; CLU_117621_6_1_9; -.
DR OMA; HYSTIKM; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0001072; F:transcription antitermination factor activity, RNA binding; IBA:GO_Central.
DR GO; GO:0060567; P:negative regulation of DNA-templated transcription, termination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
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; 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 PROSITE; PS00352; CSD_1; 1.
DR PROSITE; PS51857; CSD_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..66
FT /note="Cold shock protein CspA"
FT /id="PRO_0000262539"
FT DOMAIN 1..66
FT /note="CSD"
SQ SEQUENCE 66 AA; 7321 MW; E80AFCA652622943 CRC64;
MKQGTVKWFN AEKGFGFIEV EGENDVFVHF SAINQDGYKS LEEGQAVEFE VVEGDRGPQA
ANVVKL