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Database: UniProt
Entry: A0A161YR09_9RHOB
LinkDB: A0A161YR09_9RHOB
Original site: A0A161YR09_9RHOB 
ID   A0A161YR09_9RHOB        Unreviewed;       487 AA.
AC   A0A161YR09;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-SEP-2017, entry version 11.
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=OA90_07170 {ECO:0000313|EMBL:KZM50785.1};
OS   Labrenzia sp. OB1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Labrenzia.
OX   NCBI_TaxID=1561204 {ECO:0000313|EMBL:KZM50785.1, ECO:0000313|Proteomes:UP000076616};
RN   [1] {ECO:0000313|EMBL:KZM50785.1, ECO:0000313|Proteomes:UP000076616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OB1 {ECO:0000313|EMBL:KZM50785.1,
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: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:KZM50785.1}.
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DR   EMBL; JSEP01000004; KZM50785.1; -; Genomic_DNA.
DR   RefSeq; WP_068408964.1; NZ_JSEP01000004.1.
DR   EnsemblBacteria; KZM50785; KZM50785; OA90_07170.
DR   PATRIC; fig|1561204.3.peg.4141; -.
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   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:UP000076616};
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:UP000076616}.
FT   DOMAIN      181    310       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;  54166 MW;  48E8D9CC7A63F9CA CRC64;
     MQVQEAGGSE QWKRVKKHLR AQLGDDVFTS WFARVDLEEH QDGTVRLSVP TRFLKQWIQN
     NYNDQLMGLW QRECDNVHRI ELTVRGAIRP RQVPVSQPSL ALPSGSKPAA ADTLAEASQV
     TRAQAATAAL GRGDTGGDTP RDVLQGASLD PKYTFDTFVE GESNNLALAA ARQVASGGPV
     TFNPLYLHAA VGLGKTHLMQ AVAAKARAGG RKVLYLTAEH FMYKFVAALK SQSALAFKDT
     LRTIDLLLID DMQFLHGKQV QQEFCHTLNA LIDGARQVIV AADRAPSELD TLDDRVRSRL
     SGGLVVGIQE PDFVLRRSIL VSRVAAARKS YPQFEVPEGV LDYVARHVAS SGRDLEGALN
     RLIAHNQLTN QPITQEMAEL TLRDLVRSSE PRRVKIEDIQ RVVSKHYNVT KADLLSARRT
     RTIVRPRQIA MYLAKVMTPR SLPEIGRRFG NRDHTTVLHA VRKIEELARG DYALAQELEL
     LKRMLDA
//
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