CCPA_STAAN
ID CCPA_STAAN Reviewed; 329 AA.
AC P99175; Q99TC8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Catabolite control protein A;
GN Name=ccpA; OrderedLocusNames=SA1557;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=N315;
RX PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017;
RA Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y.,
RA Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C.,
RA Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.;
RT "Correlation of proteomic and transcriptomic profiles of Staphylococcus
RT aureus during the post-exponential phase of growth.";
RL J. Microbiol. Methods 60:247-257(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
CC -!- FUNCTION: Global transcriptional regulator of carbon catabolite
CC repression (CCR) and carbon catabolite activation (CCA), which ensures
CC optimal energy usage under diverse conditions. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB42825.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000018; BAB42825.1; ALT_INIT; Genomic_DNA.
DR PIR; D89958; D89958.
DR RefSeq; WP_000219066.1; NC_002745.2.
DR PDB; 7E5W; X-ray; 2.55 A; A/B/C=1-329.
DR PDBsum; 7E5W; -.
DR AlphaFoldDB; P99175; -.
DR SMR; P99175; -.
DR SWISS-2DPAGE; P99175; -.
DR EnsemblBacteria; BAB42825; BAB42825; BAB42825.
DR KEGG; sau:SA1557; -.
DR HOGENOM; CLU_037628_6_0_9; -.
DR Proteomes; UP000000751; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd01392; HTH_LacI; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR006377; CcpA.
DR InterPro; IPR000843; HTH_LacI.
DR InterPro; IPR046335; LacI/GalR-like_sensor.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00356; LacI; 1.
DR Pfam; PF13377; Peripla_BP_3; 1.
DR PRINTS; PR00036; HTHLACI.
DR SMART; SM00354; HTH_LACI; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR TIGRFAMs; TIGR01481; ccpA; 1.
DR PROSITE; PS00356; HTH_LACI_1; 1.
DR PROSITE; PS50932; HTH_LACI_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..329
FT /note="Catabolite control protein A"
FT /id="PRO_0000107928"
FT DOMAIN 1..57
FT /note="HTH lacI-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT DNA_BIND 5..24
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:7E5W"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:7E5W"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:7E5W"
FT HELIX 73..88
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:7E5W"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:7E5W"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:7E5W"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:7E5W"
FT HELIX 189..206
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:7E5W"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:7E5W"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:7E5W"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:7E5W"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:7E5W"
FT HELIX 291..306
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:7E5W"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:7E5W"
SQ SEQUENCE 329 AA; 36060 MW; 1D5ACFD4F34C85B4 CRC64;
MTVTIYDVAR EARVSMATVS RVVNGNQNVK AETKNKVNEV IKRLNYRPNA VARGLASKKT
TTVGVIIPDI SNIYYSQLAR GLEDIATMYK YHSIISNSDN DPEKEKEIFN NLLSKQVDGI
IFLGGTITEE MKELINQSSV PVVVSGTNGK DAHIASVNID FTEAAKEITG ELIEKGAKSF
ALVGGEHSKK AQEDVLEGLT EVLNKNGLQL GDTLNCSGAE SYKEGVKAFA KMKGNLPDAI
LCISDEEAIG IMHSAMDAGI KVPEELQIIS FNNTRLVEMV RPQLSSVIQP LYDIGAVGMR
LLTKYMNDEK IEEPNVVLPH RIEYRGTTK
