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Database: UniProt
Entry: A0A1A6L482_9VIBR
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ID   A0A1A6L482_9VIBR        Unreviewed;       466 AA.
AC   A0A1A6L482;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   16-JAN-2019, entry version 21.
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   ECO:0000313|EMBL:OBT21018.1};
GN   ORFNames=A9264_12480 {ECO:0000313|EMBL:OBT21018.1};
OS   Vibrio sp. UCD-FRSSP16_10.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=1853257 {ECO:0000313|EMBL:OBT21018.1, ECO:0000313|Proteomes:UP000092087};
RN   [1] {ECO:0000313|EMBL:OBT21018.1, ECO:0000313|Proteomes:UP000092087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-FRSSP16_10 {ECO:0000313|EMBL:OBT21018.1,
RC   ECO:0000313|Proteomes:UP000092087};
RA   Agbonavbare V., Coil D.A., Vater A.;
RT   "Draft genome sequence of Vibrio sp. UCD-FRSSP16_10.";
RL   Submitted (JUN-2016) 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:OBT21018.1}.
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DR   EMBL; LZFX01000010; OBT21018.1; -; Genomic_DNA.
DR   RefSeq; WP_068697180.1; NZ_LZFX01000010.1.
DR   EnsemblBacteria; OBT21018; OBT21018; A9264_12480.
DR   Proteomes; UP000092087; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000092087};
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:UP000092087}.
FT   DOMAIN      163    376       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      374    443       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     171    178       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      325    345       {ECO:0000256|SAM:Coils}.
FT   COILED      443    463       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   466 AA;  53026 MW;  8A85786ACB537EB0 CRC64;
     MSSSLWTQCL QQLQEELPAT EFSMWVRPLQ AELSGNTLTL FAPNRFVLDW VRDKYINSIN
     RHLQEFCDND IPSLRFEVGS KPVSAPPPIK KTAADVAAEF SAPAQLARRK PVHKTWDNDR
     DVSDITYRSN VNVKHRFNNF VEGKSNQLGL AAARQVSDNP GAAYNPLFLY GGTGLGKTHL
     LHAVGNAIVD NKPNAKVVYM HSERFVQDMV KALQNNAIEE FKRYYRSVDA LLIDDIQFFA
     NKERSQEEFF HTFNALLEGN QQIILTSDRY PKEINGVEDR LKSRFGWGLT VAIEPPELET
     RVAILMKKAE DHQIHLADEV AFFIAKRLRS NVRELEGALN RVIANANFTG RPITIDFVRE
     ALRDLLALQE KLVTIDNIQK TVAEYYKIKM ADLLSKRRSR SVARPRQLAM ALAKELTNHS
     LPEIGDAFGG RDHTTVLHAC RKIEQLKEES HDIKEDYSNL IRTLSS
//
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