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Database: UniProt
Entry: A4CLW7_ROBBH
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ID   A4CLW7_ROBBH            Unreviewed;       474 AA.
AC   A4CLW7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   25-OCT-2017, entry version 79.
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   OrderedLocusNames=RB2501_16099 {ECO:0000313|EMBL:EAR15866.1};
OS   Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Robiginitalea.
OX   NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR15866.1, ECO:0000313|Proteomes:UP000009049};
RN   [1] {ECO:0000313|EMBL:EAR15866.1, ECO:0000313|Proteomes:UP000009049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146
RC   {ECO:0000313|Proteomes:UP000009049};
RX   PubMed=19767438; DOI=10.1128/JB.01191-09;
RA   Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Robiginitalea biformata HTCC2501.";
RL   J. Bacteriol. 191:7144-7145(2009).
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: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; CP001712; EAR15866.1; -; Genomic_DNA.
DR   RefSeq; WP_015755181.1; NC_013222.1.
DR   ProteinModelPortal; A4CLW7; -.
DR   STRING; 313596.RB2501_16099; -.
DR   EnsemblBacteria; EAR15866; EAR15866; RB2501_16099.
DR   KEGG; rbi:RB2501_16099; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000009049; 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; IPR024633; DnaA_N_dom.
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   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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000009049};
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:UP000009049}.
FT   DOMAIN      172    302       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      383    452       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     180    187       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   474 AA;  54238 MW;  FAAF2C71AA8E3658 CRC64;
     MNVTANSVWK NCLAFIEDNI QPQAFKTWFV PIKPVKLSEK ALSIQVPSKF FYEWLEEHYV
     KLLKVALTRE LGEGAKLVYV IKMENTYGNR EPFTEKIPSA NRGQMTPQEM DVPIKSKNPE
     LKNPFVIPGI RNIKIESQLN PSYNFENFLE GDSNRLARSA GMAVANKPGG TSFNPLLVFG
     GVGLGKTHLA HAIGVEIKDK YPERTVLYIS AEKFTQQYIE SVRKNTRNDF IHFYQLIDVL
     IIDDVQFLSG KSGTQDVFFH IFNHLHQNGK QVILTSDKAP VDMQDIEQRL LSRFKWGLSA
     ELQSPDYETR VCILKNKLYR DGVEMPEEII DYVAKHIKSN IRELEGAIIS LIAQSSFNKK
     EVTLDLAQQV VEKFVKNTKR EVSIEYIQKV VSDYFEMDVA TLQSKTRKRH IVQARQLAMF
     FAKKFTKASL ASIGSQIGKR DHATVLHACK TVDNLAETDK QFRKYIEDLT KKFS
//
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