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Database: UniProt
Entry: D9QD56_CORP2
LinkDB: D9QD56_CORP2
Original site: D9QD56_CORP2 
ID   D9QD56_CORP2            Unreviewed;       603 AA.
AC   D9QD56;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   25-OCT-2017, entry version 51.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:ADL09500.1};
GN   OrderedLocusNames=CpC231_0001 {ECO:0000313|EMBL:ADL09500.1};
OS   Corynebacterium pseudotuberculosis (strain C231).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL09500.1, ECO:0000313|Proteomes:UP000000276};
RN   [1] {ECO:0000313|EMBL:ADL09500.1, ECO:0000313|Proteomes:UP000000276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C231 {ECO:0000313|EMBL:ADL09500.1,
RC   ECO:0000313|Proteomes:UP000000276};
RX   PubMed=21037006; DOI=10.1128/JB.01211-10;
RG   Consortium: Rede Paraense de Genomica e Proteomica (RPGP);
RA   Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T.,
RA   Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S.,
RA   Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F.,
RA   de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.;
RT   "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a
RT   strain isolated from a cow in Israel with bovine mastitis.";
RL   J. Bacteriol. 193:323-324(2011).
RN   [2] {ECO:0000313|EMBL:ADL09500.1, ECO:0000313|Proteomes:UP000000276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C231 {ECO:0000313|EMBL:ADL09500.1,
RC   ECO:0000313|Proteomes:UP000000276};
RX   PubMed=21533164; DOI=10.1371/journal.pone.0018551;
RA   Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R.,
RA   Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P.,
RA   Turk M.Z., Seyffert N., Moraes P.M., Soares S.C., Almeida S.S.,
RA   Castro T.L., Abreu V.A., Trost E., Baumbach J., Tauch A.,
RA   Schneider M.P., McCulloch J., Cerdeira L.T., Ramos R.T., Zerlotini A.,
RA   Dominitini A., Resende D.M., Coser E.M., Oliveira L.M., Pedrosa A.L.,
RA   Vieira C.U., Guimaraes C.T., Bartholomeu D.C., Oliveira D.M.,
RA   Santos F.R., Rabelo E.M., Lobo F.P., Franco G.R., Costa A.F.,
RA   Castro I.M., Dias S.R., Ferro J.A., Ortega J.M., Paiva L.V.,
RA   Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P., Falcao P.R.,
RA   Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C.,
RA   Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.;
RT   "Evidence for reductive genome evolution and lateral acquisition of
RT   virulence functions in two Corynebacterium pseudotuberculosis
RT   strains.";
RL   PLoS ONE 6:E18551-E18551(2011).
CC   -!- FUNCTION: Plays an important role in the initiation and regulation
CC       of chromosomal replication. Binds to the origin of replication; it
CC       binds specifically double-stranded DNA at a 9 bp consensus (dnaA
CC       box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic
CC       phospholipids. {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00735475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
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DR   EMBL; CP001829; ADL09500.1; -; Genomic_DNA.
DR   RefSeq; WP_014400874.1; NC_017301.1.
DR   EnsemblBacteria; ADL09500; ADL09500; CpC231_0001.
DR   GeneID; 12298869; -.
DR   KEGG; cpq:CpC231_0001; -.
DR   PATRIC; fig|681645.3.peg.1; -.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   Proteomes; UP000000276; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   HAMAP; MF_00377; DnaA_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001957; Chromosome_initiator_DnaA.
DR   InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR   InterPro; IPR018312; Chromosome_initiator_DnaA_CS.
DR   InterPro; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF2; PTHR30050:SF2; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF08299; Bac_DnaA_C; 1.
DR   PRINTS; PR00051; DNAA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00760; Bac_DnaA_C; 1.
DR   SUPFAM; SSF48295; SSF48295; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00362; DnaA; 1.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000276};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000276}.
FT   DOMAIN      290    418       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      507    576       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     298    305       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   603 AA;  67697 MW;  7B27FEDE0A92A00C CRC64;
     MSEAPSTWNE RWQEVTNELL SQSQDPESGI SITRQQSAYL RLVKPVAFVE GIAVLSVPHA
     RAKKEIETTL GPVITEVLSR RLGRQYSLAV SVHAPEENPE VSSATPDAVS YYQEQSAVSG
     QYGATSANAD FQNQQSTIYR KPQESQYPVT FGASSYGNEK YQENSQDQGI SHHPYGFNEA
     QRIASSASHA VPQSGSELLH DPVHTRRTDA ALDQNYPGNT GGWRTEHIQE PMPTEQIPSG
     TPRTREQPSF NPDRALALNP HYTFDSYVVS DSNKLPCSAA IAVAEKPARA YNPLFIWGDS
     GLGKTHLMHA VGNYAQYLNP RLRIKYVSSE EFTNEYINSV RDDRQEAFKR KYRELDILMV
     DDIQFLQGKE GTQEEFFHTF NALYQANKQI VLSSDRPPKQ LTTLEDRLRT RFQAGLIADI
     YPPDLETRIA ILMKKAASES IVADREAIEL IASRFNTSIR ELEGAFIRVS AYASLMSPDK
     GKHRIDLRIA EKALEDMMPE QANEEITATT ILAATAEYFE MDVNALKGSG KTRAVAHARQ
     LAMYLCRELT DLSLPKIGEQ FGGKDHTTVM YADRKIRKEI TEKKETYDEI QLLTQQIKSS
     SRG
//
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