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Database: UniProt
Entry: K0C2V0_CYCSP
LinkDB: K0C2V0_CYCSP
Original site: K0C2V0_CYCSP 
ID   K0C2V0_CYCSP            Unreviewed;       441 AA.
AC   K0C2V0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   05-JUL-2017, entry version 35.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:AFT66042.1};
GN   OrderedLocusNames=Q91_0001 {ECO:0000313|EMBL:AFT66042.1};
OS   Cycloclasticus sp. (strain P1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Cycloclasticus.
OX   NCBI_TaxID=385025 {ECO:0000313|EMBL:AFT66042.1, ECO:0000313|Proteomes:UP000006282};
RN   [1] {ECO:0000313|EMBL:AFT66042.1, ECO:0000313|Proteomes:UP000006282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1 {ECO:0000313|EMBL:AFT66042.1,
RC   ECO:0000313|Proteomes:UP000006282};
RX   PubMed=23144416; DOI=10.1128/JB.01837-12;
RA   Lai Q., Li W., Wang B., Yu Z., Shao Z.;
RT   "Complete genome sequence of the pyrene-degrading bacterium
RT   Cycloclasticus sp. strain P1.";
RL   J. Bacteriol. 194:6677-6677(2012).
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:SAAS00724167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00756131}.
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; CP003230; AFT66042.1; -; Genomic_DNA.
DR   RefSeq; WP_015004814.1; NC_018697.1.
DR   EnsemblBacteria; AFT66042; AFT66042; Q91_0001.
DR   KEGG; cyq:Q91_0001; -.
DR   PATRIC; fig|385025.3.peg.1; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000006282; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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; IPR024633; DnaA_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF12; PTHR30050:SF12; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF08299; Bac_DnaA_C; 1.
DR   Pfam; PF11638; DnaA_N; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006282};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006282}.
FT   DOMAIN      138    269       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      349    418       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     146    153       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   441 AA;  50014 MW;  51567F4A5CA294C4 CRC64;
     MSSLWEQCLQ RLEEEIPPQQ INTWVRPLQA QTNNDELLLF APNKFVLDWV SDNYIENITN
     IINKLTENKI KLHLKIGSSK VQPSPATVSK KTTTKANNTP SVSHNLNSAF TFDSFVMGKS
     NELAKAAAIQ VSENPGVSYN PLFIYGGVGL GKTHLMHSIG NAILQKNKNK RVSFLSSERF
     VSGMVQSLQK NTINDFKNYY RSLDLLLIDD IQFFAKKERS QEEFFHTFNT LIENNKQIVL
     TCDCYPKEIN GLEERLKSRF GWGLPIPIEP PDLETRVAIL KSKAALSGVD LADEVAFFMG
     NRIKSNVREL EGALRRVLAN ANFTGKPITL DFTKEALRDL IALQNKRISI DNIQKTVAEY
     YKIRTSDLLS AKRTRSIARP RQIAMALAKE LTQYSLPEIG NQFGGRDHTT VLHATRKVKE
     LRDSDQLIDE DYINLLRTLS H
//
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