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Database: UniProt
Entry: A0A0F3H222_9BACT
LinkDB: A0A0F3H222_9BACT
Original site: A0A0F3H222_9BACT 
ID   A0A0F3H222_9BACT        Unreviewed;       444 AA.
AC   A0A0F3H222;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   05-JUL-2017, entry version 16.
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=MBAV_000839 {ECO:0000313|EMBL:KJU86968.1};
OS   Candidatus Magnetobacterium bavaricum.
OC   Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae;
OC   Candidatus Magnetobacterium.
OX   NCBI_TaxID=29290 {ECO:0000313|EMBL:KJU86968.1, ECO:0000313|Proteomes:UP000033423};
RN   [1] {ECO:0000313|EMBL:KJU86968.1, ECO:0000313|Proteomes:UP000033423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM-1 {ECO:0000313|EMBL:KJU86968.1};
RA   Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT   "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT   conserved set of magnetosome genes.";
RL   Submitted (FEB-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:SAAS00756131}.
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:KJU86968.1}.
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DR   EMBL; LACI01000381; KJU86968.1; -; Genomic_DNA.
DR   EnsemblBacteria; KJU86968; KJU86968; MBAV_000839.
DR   PATRIC; fig|29290.4.peg.1105; -.
DR   Proteomes; UP000033423; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033423};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033423}.
FT   DOMAIN      141    269       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      352    421       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     149    156       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   444 AA;  50374 MW;  ACD05447ED0678C8 CRC64;
     MDLEKIWHDS LMIVQSQVTE SVFELWFKPI RLFNLEGTEA VLVVPNRFFG DWVDDNYPGL
     LNEALSEVVS SPITLQFRVD TDQHGDEQVK KDLIQQAKKV RTAGKGIYLN VKYTFESFVV
     GASNQFAHAA ALAVSESLGR AYNPLFIYGD VGLGKTHLIN AIGNKVIKRL STATVLYVSS
     EQFTNEVVSA IRHEKMSELK DRYRSLDMLL IDDVQFIANK TQTQEEFFHT FNALYERQKQ
     IVISSDRPPK ELGAITDRLK SRFTMGLIAD IQQPTVEHKI AILQRKAEDQ KILLPDDVTY
     YMASRVRSNI RELEGCLIKL AAHSNLTGQP ISVAVAKNVL KDLFYDDIKP INIENIQKMV
     CEYYGIKLTD IKAKKRTKEL IIPRQLAMYI SKQLTDLSLG DIGKAFGGKD HATVIYACKQ
     VEAKIKKDEG FNKVVQQIIN RIKP
//
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