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Database: UniProt
Entry: A0A1V9FSQ5_9BACT
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Original site: A0A1V9FSQ5_9BACT 
ID   A0A1V9FSQ5_9BACT        Unreviewed;       477 AA.
AC   A0A1V9FSQ5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   13-FEB-2019, entry version 13.
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   ORFNames=A3860_06830 {ECO:0000313|EMBL:OQP61419.1};
OS   Niastella vici.
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales;
OC   Chitinophagaceae; Niastella.
OX   NCBI_TaxID=1703345 {ECO:0000313|EMBL:OQP61419.1, ECO:0000313|Proteomes:UP000192796};
RN   [1] {ECO:0000313|EMBL:OQP61419.1, ECO:0000313|Proteomes:UP000192796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ57 {ECO:0000313|EMBL:OQP61419.1,
RC   ECO:0000313|Proteomes:UP000192796};
RA   Chen L., Wang D., Yang S., Wang G.;
RT   "Niastella vici sp. nov., isolated from farmland soil.";
RL   Submitted (MAR-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:OQP61419.1}.
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DR   EMBL; LVYD01000058; OQP61419.1; -; Genomic_DNA.
DR   BioCyc; GCF_002077945:A3860_RS27125-MONOMER; -.
DR   Proteomes; UP000192796; 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   Complete proteome {ECO:0000313|Proteomes:UP000192796};
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:UP000192796}.
FT   DOMAIN      171    301       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      382    451       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     179    186       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   477 AA;  55163 MW;  4E2965F4F7193C59 CRC64;
     MAKTSEKVWS NCLEIIKDIV EWQHFKTWFE PIKPVELRDN ILIIQVPSQF FYEYLEEHYV
     NLLAKTLRRV LGKDARLEYR IMVDSGNHNN KPLTMDVPTH GYKTFSSNEM DFPLIINNPV
     KNPFVIPGLK KMQIDPQLNP IYTFENFIEG DCNRVARRAG KTVAEKPGAS SFNPLVIYGG
     VGLGKTHLAQ GIGNETKRLH PNKVVLYVSS EKFINQFQDH SRNNAINDFI HFYQLIDVLI
     IDDVQFFNRA EKSQDAFFAI FNHLHQSGKQ LILTSDKPPK DLEGVQERLL SRFRWGLSAD
     LQVPDYETRI EILERKMKND GLEMPKEVVK YLAYNINSNV RELEGALISL LAQSSLNKRE
     IDLDLAKRVL RNFVKTSSKE ITIETIQKMV CEYFDVPYDK LLQKTRKREI VQARQITMYL
     AKAFTKNSLK TIGEHFGGRD HTTVIHSCQT VKDLMDTDST FRESVMELQQ KVQLAAM
//
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