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Database: UniProt
Entry: C6RJ24_9PROT
LinkDB: C6RJ24_9PROT
Original site: C6RJ24_9PROT 
ID   C6RJ24_9PROT            Unreviewed;       436 AA.
AC   C6RJ24;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   05-JUL-2017, entry version 50.
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:EET78605.1};
GN   ORFNames=CAMSH0001_0120 {ECO:0000313|EMBL:EET78605.1};
OS   Campylobacter showae RM3277.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=553219 {ECO:0000313|EMBL:EET78605.1, ECO:0000313|Proteomes:UP000003107};
RN   [1] {ECO:0000313|EMBL:EET78605.1, ECO:0000313|Proteomes:UP000003107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM3277 {ECO:0000313|EMBL:EET78605.1,
RC   ECO:0000313|Proteomes:UP000003107};
RA   Madupu R., Sebastian Y., Durkin A.S., Torralba M., Methe B.,
RA   Sutton G.G., Strausberg R.L., Nelson K.E.;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EET78605.1}.
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DR   EMBL; ACVQ01000033; EET78605.1; -; Genomic_DNA.
DR   RefSeq; WP_004321713.1; NZ_ACVQ01000033.1.
DR   STRING; 553219.CAMSH0001_0120; -.
DR   EnsemblBacteria; EET78605; EET78605; CAMSH0001_0120.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   Proteomes; UP000003107; Unassembled WGS sequence.
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:UP000003107};
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:UP000003107}.
FT   DOMAIN      133    259       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      342    411       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     141    148       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   436 AA;  50144 MW;  D0B56FC670001C47 CRC64;
     MVANEVLELL SKEILPSEFE CYIKQLKFNE KSSNSTNVVF NAPNEIIAKF IQTKYASKIA
     HLFEVKTGQK PVINVQAATK TQSKPAKKVD VKEIKAQSSL LNPSYTFENF VVGDSNQFAF
     LSAKAVSEQL GKIYNPLFIY GPTGLGKTHL LQSVGNFCLN GGKMVICVTS EQFITDFTYN
     LNNHSMERFR EKYRNCDVLL IDDVQFLGKT DKIQEEFFHT FNELHAKNGQ IVMTSDRQPK
     LLKGFEDRLR TRFEWGIIAD ITPPELDTKI AIIKKKCEFD KIYLDKDVIN YIATNMGDNI
     REIESAIINL NAYARLMRQE ITLEFAKNIL RDQIKEKREN INLENIVEIV SKELNVKPSE
     MKSKSRSKNI VEARRIVIYL AKNLTPNSMP QIAQFFNMKD HSAVSHSIKK INELIETNEY
     FKVRVEELKN KILTKE
//
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