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Database: UniProt
Entry: V2UPV8_9GAMM
LinkDB: V2UPV8_9GAMM
Original site: V2UPV8_9GAMM 
ID   V2UPV8_9GAMM            Unreviewed;       465 AA.
AC   V2UPV8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   25-OCT-2017, entry version 30.
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=P255_02649 {ECO:0000313|EMBL:ESK50661.1};
OS   Acinetobacter brisouii CIP 110357.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=1341683 {ECO:0000313|EMBL:ESK50661.1, ECO:0000313|Proteomes:UP000018418};
RN   [1] {ECO:0000313|EMBL:ESK50661.1, ECO:0000313|Proteomes:UP000018418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 110357 {ECO:0000313|EMBL:ESK50661.1,
RC   ECO:0000313|Proteomes:UP000018418};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA   Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA   McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA   Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter brisouii CIP 110357.";
RL   Submitted (OCT-2013) 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:SAAS00911680}.
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:ESK50661.1}.
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DR   EMBL; AYEU01000007; ESK50661.1; -; Genomic_DNA.
DR   RefSeq; WP_004902965.1; NZ_KI530763.1.
DR   EnsemblBacteria; ESK50661; ESK50661; P255_02649.
DR   PATRIC; fig|1341683.3.peg.2618; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000018418; 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: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:UP000018418};
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:UP000018418}.
FT   DOMAIN      162    292       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      373    442       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     170    177       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   465 AA;  52491 MW;  EF0E141A2CF70B0A CRC64;
     MLWTDCLTRL RQELSDNVFA MWIRPLVAEE HEHTLRLYAP NPYWTRYIQE HHLELISILA
     EQLSEGRIRH VEIMVDSRPG AILKASEQPA TTVSALETPA PSIAKKEKEP EIPSIAQPVA
     AKLSKKRQLN PLFTFSLFVE GRSNQMAAET CRKVLTQLGA SQHNPLFLYG PTGLGKTHLM
     QAVGNALLQA KPNARVMYMT AESFVQDFVS SLQKGKVEEF KKNCRSLDLL LVDDIHLLAG
     KEASLVEFFY TFNALLDESK QIILTSDRYP KELTELDPRL VSRFSWGLSV GVEPPDIETR
     IEILLKKAES TGVDLPRNCA LFIAQQVVAN VRELEGALNK VVAISRFKGS AIDLDVVRES
     LKDVLAIRAR TISTENIQRV VSEYFRIPLK ELIGPKRTRI YARPRQLAMG LARELTGDSF
     PEIGMAFGGR DHSTVMHACE KVQSLREEDP IFDEDYKNLT RLLQS
//
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