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Database: UniProt
Entry: A0A0J1GZG6_9GAMM
LinkDB: A0A0J1GZG6_9GAMM
Original site: A0A0J1GZG6_9GAMM 
ID   A0A0J1GZG6_9GAMM        Unreviewed;       466 AA.
AC   A0A0J1GZG6;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   25-OCT-2017, entry version 18.
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   ECO:0000313|EMBL:KLV05046.1};
GN   ORFNames=ABT57_22515 {ECO:0000313|EMBL:KLV05046.1};
OS   Photobacterium ganghwense.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=320778 {ECO:0000313|EMBL:KLV05046.1, ECO:0000313|Proteomes:UP000035909};
RN   [1] {ECO:0000313|EMBL:KLV05046.1, ECO:0000313|Proteomes:UP000035909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22954 {ECO:0000313|EMBL:KLV05046.1,
RC   ECO:0000313|Proteomes:UP000035909};
RA   Machado H., Gram L.;
RT   "Photobacterium galathea sp. nov.";
RL   Submitted (MAY-2015) 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:KLV05046.1}.
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DR   EMBL; LDOU01000028; KLV05046.1; -; Genomic_DNA.
DR   RefSeq; WP_047887509.1; NZ_LDOU01000028.1.
DR   EnsemblBacteria; KLV05046; KLV05046; ABT57_22515.
DR   PATRIC; fig|320778.3.peg.4827; -.
DR   Proteomes; UP000035909; 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:UP000035909};
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:UP000035909}.
FT   DOMAIN      163    365       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}.
SQ   SEQUENCE   466 AA;  52942 MW;  C606BA2A7A6625CB CRC64;
     MSSSLWLQCL QRLQEELPAT EFSMWVRPLQ AELNDNTLTL FAPNRFVLDW VRDKYLNNIN
     RLLNEFCGND VPILRFEVGS RPVTAPPPQP AVIPASLQPA PGIIDEPPSR RWEPAPSPVQ
     PESQAGYRSN VNPKHNFNNF VEGKSNQLGL AACRQVADNP GAAYNPLFLY GGTGLGKTHL
     LHAVGNAIAD RKPNAKVVYM HSERFVQDMV KALQNNAIEE FKRYYRSVDA LLIDDIQFFA
     NKERSQEEFF HTFNALLEGN QQIILTSDRY PREINGVEDR LKSRFGWGLT VAIEPPELET
     RVAILMKKAE DHNIRLADEV AFFIAKRLRS NVRELEGALN RVIANANFTG RAITIDFVRE
     ALRDLLALQE KLVTIDNIQK TVAEYYKIKM ADMLSKRRSR SVARPRQMAM ALAKELTNHS
     LPEIGDAFGG RDHTTVLHAC RKIEQLREES HDIKEDYSNL IRTLSS
//
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