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Database: UniProt
Entry: A0A161YT08_9RHOB
LinkDB: A0A161YT08_9RHOB
Original site: A0A161YT08_9RHOB 
ID   A0A161YT08_9RHOB        Unreviewed;       487 AA.
AC   A0A161YT08;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 19.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=OA90_03305 {ECO:0000313|EMBL:KZM51705.1};
OS   Labrenzia sp. OB1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Labrenzia.
OX   NCBI_TaxID=1561204 {ECO:0000313|EMBL:KZM51705.1, ECO:0000313|Proteomes:UP000076616};
RN   [1] {ECO:0000313|EMBL:KZM51705.1, ECO:0000313|Proteomes:UP000076616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OB1 {ECO:0000313|EMBL:KZM51705.1,
RC   ECO:0000313|Proteomes:UP000076616};
RA   Paerl R.W., Allen E., Palenik B., Azam F.;
RT   "Marine bacterioplankton release vitamin B1 sources.";
RL   Submitted (OCT-2014) 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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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:KZM51705.1}.
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DR   EMBL; JSEP01000002; KZM51705.1; -; Genomic_DNA.
DR   RefSeq; WP_068407787.1; NZ_JSEP01000002.1.
DR   EnsemblBacteria; KZM51705; KZM51705; OA90_03305.
DR   PATRIC; fig|1561204.3.peg.2196; -.
DR   Proteomes; UP000076616; 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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000076616};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076616}.
FT   DOMAIN      181    325       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      395    464       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     189    196       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   487 AA;  54133 MW;  7D367BF80DD39414 CRC64;
     MQLQALADSG PWDRVKKELR NELGEDIFSN WFGRVNHEET TGDAVRLSVP TRFLKNWIQS
     NYEKQLVGLW KREKDGISRI ELTVRGALRP RLIEGPQASK AITARRISGR PAPFNSTPQF
     SAGSGIAAIP CLADTGEESA SEFLSGAALN PKLTFDTFAE GTSNSLACAA VRQMAAGHEG
     TLNMLYVHSS TGIGKTHLLQ AAACQARKTG RHVAYLSAEF FMYHLVPALR TPAFPVLRQA
     MKSIDLLLID DLQFLHGKQA QEEFSKTLEL LMEFPSQVIM AADRAPEDLE TLGTGLCQYI
     QKGEVIGIQA TDYALRLDIV NKRIAAARKT HPGFSVPDEV TDYIARYVIA SARDLEGALN
     RLFAHNQLSR QPVTLELAEK TLHDLVRIGE PRSIKVEEIQ QVVCKHFSVT KADLLSSCRA
     RVLVRPRQIA MYIAKVMTGR SLPEIGRRFG NRDHTTVLHA VRKIDSMVKT DRALSQEVEL
     LKRLIQS
//
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