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Database: UniProt
Entry: N9GVR1_ACIHA
LinkDB: N9GVR1_ACIHA
Original site: N9GVR1_ACIHA 
ID   N9GVR1_ACIHA            Unreviewed;       464 AA.
AC   N9GVR1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   25-OCT-2017, entry version 34.
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=F927_00376 {ECO:0000313|EMBL:ENW21336.1};
OS   Acinetobacter haemolyticus CIP 64.3.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=1217659 {ECO:0000313|EMBL:ENW21336.1, ECO:0000313|Proteomes:UP000017667};
RN   [1] {ECO:0000313|EMBL:ENW21336.1, ECO:0000313|Proteomes:UP000017667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 64.3 {ECO:0000313|EMBL:ENW21336.1,
RC   ECO:0000313|Proteomes:UP000017667};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter haemolyticus CIP 64.3.";
RL   Submitted (FEB-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:ENW21336.1}.
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DR   EMBL; APQQ01000005; ENW21336.1; -; Genomic_DNA.
DR   RefSeq; WP_005086074.1; NZ_KB849808.1.
DR   EnsemblBacteria; ENW21336; ENW21336; F927_00376.
DR   PATRIC; fig|1217659.3.peg.365; -.
DR   Proteomes; UP000017667; 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:UP000017667};
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:UP000017667}.
FT   DOMAIN      161    291       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      372    441       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     169    176       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   464 AA;  52355 MW;  A2F3A59FECB20DF3 CRC64;
     MLWTDCLTRL RQELSDNVFA MWIRPLVAEE VDDVMRLYAP NPYWTRYIQD NHLELISILA
     EQLSEGRVRQ VEILVDSRPG TILASSEQPA TTTAALNTST PIPTKIKKEA DLVQPSQNAN
     KIPKKRQLNP LFTFSLFVEG RSNQMAAETC RKVLTQLGAS QHNPLFLYGP TGLGKTHLMQ
     AVGNALLQAK PNARVMYMTS ESFVQDFVSS LQKGKVEEFK KNCRSLDLLL VDDIHLLAGK
     EASLVEFFYT FNALLDESKQ IILTSDRYPK ELTELDPRLV SRFSWGLSVG VEPPDIETRI
     EILLKKAENS GVDLPRNCAL FIAQQVVANV RELEGALNKV VAISRFKGTA IDLDVVRESL
     KDVLAIRART ISVENIQRVV SEYFRIPLKE LIGPKRTRIY ARPRQLAMGL ARELTGDSFP
     EIGMAFGGRD HSTVMHACEK VVSLREEDPI FNEDYKNLLR LLQS
//
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