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Database: UniProt
Entry: A2U477_9FLAO
LinkDB: A2U477_9FLAO
Original site: A2U477_9FLAO 
ID   A2U477_9FLAO            Unreviewed;       475 AA.
AC   A2U477;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-SEP-2017, entry version 72.
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:EAQ41037.1};
GN   ORFNames=MED152_13404 {ECO:0000313|EMBL:EAQ41037.1};
OS   Polaribacter sp. MED152.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Polaribacter.
OX   NCBI_TaxID=313598 {ECO:0000313|EMBL:EAQ41037.1, ECO:0000313|Proteomes:UP000006470};
RN   [1] {ECO:0000313|EMBL:EAQ41037.1, ECO:0000313|Proteomes:UP000006470}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED152 {ECO:0000313|EMBL:EAQ41037.1};
RX   PubMed=17215843; DOI=10.1038/nature05381;
RA   Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P.,
RA   Pascher T., Neutze R., Pedros-Alio C., Pinhassi J.;
RT   "Light stimulates growth of proteorhodopsin-containing marine
RT   Flavobacteria.";
RL   Nature 445:210-213(2007).
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; CP004349; EAQ41037.1; -; Genomic_DNA.
DR   RefSeq; WP_015482402.1; NC_020830.1.
DR   ProteinModelPortal; A2U477; -.
DR   STRING; 313598.MED152_13404; -.
DR   EnsemblBacteria; EAQ41037; EAQ41037; MED152_13404.
DR   KEGG; pom:MED152_13404; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000006470; 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: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:UP000006470};
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:UP000006470}.
FT   DOMAIN      172    308       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   475 AA;  54505 MW;  894C27D1542B48DF CRC64;
     MSYTAESVWT DCLSFIKDNI KPQAYKTWFE PIKPVKLSGE ALTIQVPSKF FYEWLEEHYI
     KLLRVALVRQ LGNDAKLIYD VKMENNYSSN RPQIVKIPSS NRDPLKPQRV TVPLESNKRE
     LRNPFIIPGL QKVKIESQLN PNYSFANFVE GDSNRLARSA GMAVANKPGG TSFNPLLIYG
     GVGLGKTHLS HAIGVDIKDK YPDKTVLYIS SEKFTQQFID SVKSNTRNDF IHFYQMIDVL
     IIDDVQFLSG KAGTQDVFFH IFNHLHQNGK QVILTSDKAP VDMQDIEQRL LSRFKWGLSA
     ELQAPDYETR ISILQNKLFR DGVEMPEEII EYIAKNIKSN VRELEGVIIS MIAQASFNRR
     EFSIELAKQI VDKFVKNTKK EVSIDYIQKE VSKYFDMDVA TLQSKTRKRH IVQARQLAMF
     FAKRLTKTSL ASIGNQIGQR DHATVLHACK TVDNLTETDK QFKKYVDDLT KKLTF
//
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