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Database: UniProt
Entry: A0A124FVV3_9FIRM
LinkDB: A0A124FVV3_9FIRM
Original site: A0A124FVV3_9FIRM 
ID   A0A124FVV3_9FIRM        Unreviewed;       446 AA.
AC   A0A124FVV3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   05-JUL-2017, entry version 11.
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=XD91_1010 {ECO:0000313|EMBL:KUK72910.1};
OS   Clostridiales bacterium 38_11.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales.
OX   NCBI_TaxID=1641393 {ECO:0000313|EMBL:KUK72910.1, ECO:0000313|Proteomes:UP000053314};
RN   [1] {ECO:0000313|EMBL:KUK72910.1, ECO:0000313|Proteomes:UP000053314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=38_11 {ECO:0000313|EMBL:KUK72910.1};
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-resolved metagenomic analysis reveals roles for candidate
RT   phyla and other microbial community members in biogeochemical
RT   transformations in oil reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK72910.1}.
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DR   EMBL; LGGM01000037; KUK72910.1; -; Genomic_DNA.
DR   PATRIC; fig|1641393.3.peg.1259; -.
DR   Proteomes; UP000053314; 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:UP000053314};
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:UP000053314}.
FT   DOMAIN      144    272       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      355    424       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     152    159       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   446 AA;  51371 MW;  F65B96AAFDC9088B CRC64;
     MNNSIAQLWD EVLAIIKEDM NEVSYNTWLK PIKPLHINNN VIYLQAPEEF LRDMLVKRYN
     NLLKNAFTYV LNDNEISIKI LIPDEEIDEQ KMVEKRDKNF TYQNGNTIKS FLNPKYKFDS
     FIVGNSNRFA HAASLAVAEA PATAYNPLFL YGGVGLGKTH LMHAIGHYIM SNNKDSKILY
     VTSEKFTNDL INSIKDDKNE AFRNKYRKID VLLVDDIQFI AGKERTQEEF FHTFNALHND
     NKQIIISSDR PPKEILTLED RLRSRFEMGL TADVQTPDLE TRIAILRKKA EDEKYDVSDE
     IIEYIANNIQ SNIRKLEGAL IRLYAYSSLT NKEVTMELAY EALKHLISDK NKLITIDLIK
     NAISNYFNIS LEDLSSKKKP KSISHPRQVA MYLSRKHTDN SLPKIGDEFG GRDHSTVIHA
     FNKITADLET DNELKKAIED LEAELL
//
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