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Database: UniProt
Entry: K2I4I6_9RHOB
LinkDB: K2I4I6_9RHOB
Original site: K2I4I6_9RHOB 
ID   K2I4I6_9RHOB            Unreviewed;       469 AA.
AC   K2I4I6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-SEP-2017, entry version 34.
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   ORFNames=OCGS_2134 {ECO:0000313|EMBL:EKE43800.1};
OS   Oceaniovalibus guishaninsula JLT2003.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Oceaniovalibus.
OX   NCBI_TaxID=1231392 {ECO:0000313|EMBL:EKE43800.1, ECO:0000313|Proteomes:UP000006765};
RN   [1] {ECO:0000313|EMBL:EKE43800.1, ECO:0000313|Proteomes:UP000006765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLT2003 {ECO:0000313|EMBL:EKE43800.1,
RC   ECO:0000313|Proteomes:UP000006765};
RX   PubMed=23144420; DOI=10.1128/JB.01874-12;
RA   Tang K., Liu K., Jiao N.;
RT   "Draft Genome Sequence of Oceaniovalibus guishaninsula JLT2003T.";
RL   J. Bacteriol. 194:6683-6683(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}.
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:EKE43800.1}.
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DR   EMBL; AMGO01000047; EKE43800.1; -; Genomic_DNA.
DR   EnsemblBacteria; EKE43800; EKE43800; OCGS_2134.
DR   PATRIC; fig|1231392.3.peg.2146; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000006765; Unassembled WGS sequence.
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; 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:UP000006765};
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:UP000006765}.
FT   DOMAIN      159    289       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      376    445       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     167    174       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   469 AA;  52802 MW;  C1C8FCFC2BAB0CC2 CRC64;
     MQKGDRRMTR DSWGIVKQDL KLKVGHNNFV TWIEPLEFGS LDDGILTFRV PSMFIGNWVS
     RYFCDQIIDE ANARGAGVRR LAFVVGEPAN RPVPCNGEPD AAPADKAPAP ARTAAPASGM
     TITGARLNEN YTFDAFVVGK PNELAYSAAR RVAEGGPVTF NPLFLYGGVG LGKTHLMNAI
     AWELRARDPG ARVLYMSAEQ FMYRFVQALR DRQMIDFKQI FRSVDVLMVD DVQFIAGKDS
     TQEEFFHTFN ALIEQGKQII ISADTAPGEI SGLERRVVSR LQSGLVVDLH PTSYELRLGI
     LQRKVEQFRD QFAGVRIGEG VLEMVAHRIT SNVRELEGAL MRLFAFGSLI DRGEVDQEAT
     RECLSDLMRT YDRRASIDEI QRKVADHYNI RISDLVGPKR TRIYSRPRQV AMFLAKEFTD
     RSLPEIGRRF GGRDHTTILH GIRAIAKLCD TDSQTAEDVD MLRRVLRDI
//
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