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Database: UniProt
Entry: F0GYV2_9FIRM
LinkDB: F0GYV2_9FIRM
Original site: F0GYV2_9FIRM 
ID   F0GYV2_9FIRM            Unreviewed;       458 AA.
AC   F0GYV2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   25-OCT-2017, entry version 43.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:EGC84592.1};
GN   ORFNames=HMPREF9246_1510 {ECO:0000313|EMBL:EGC84592.1};
OS   Anaerococcus hydrogenalis ACS-025-V-Sch4.
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Anaerococcus.
OX   NCBI_TaxID=879306 {ECO:0000313|EMBL:EGC84592.1, ECO:0000313|Proteomes:UP000005277};
RN   [1] {ECO:0000313|EMBL:EGC84592.1, ECO:0000313|Proteomes:UP000005277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-025-V-Sch4 {ECO:0000313|EMBL:EGC84592.1,
RC   ECO:0000313|Proteomes:UP000005277};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JAN-2011) 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:SAAS00735475}.
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:EGC84592.1}.
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DR   EMBL; AEXN01000010; EGC84592.1; -; Genomic_DNA.
DR   RefSeq; WP_004816343.1; NZ_AEXN01000010.1.
DR   EnsemblBacteria; EGC84592; EGC84592; HMPREF9246_1510.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000005277; 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; 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   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:UP000005277};
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}.
FT   DOMAIN      155    289       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      367    435       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     163    170       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   458 AA;  53199 MW;  557F012AE0E0FC98 CRC64;
     MNLEYITNEL KEKMKMNVPD LQQYETWIGI LKPLNKYDNT IYLEIPKNDT KFIFDQIWVP
     QLQAILNDIN KRESTSYKVE IVAKDGPNYE DILTLGRNVD DNGQLRLNNV NRYPKPLLEK
     NNIFENFVQG KSNQLALAAS QSVAENMANY KVSRVYNPLF IYGSSGLGKT HLMQAIAHEI
     LKKRDDCYVM YLSSEKFTNE MISAVRNNTN EEFRKKYRSV DMLLIDDIQF IANKTGTQEE
     FFHTFEDLYN QGKQIVISSD RPPKEIKHLE ERLVSRFGWG IIVDISKPDF ETRVAILQKK
     QDELGAVVDY KILEYIAENI ETNIRDLEGA LATSIACAKS NNRSYVSLED ARLGVSSRVH
     KDKKQISAED IQKKVSDRYH VKLTDLRGKS RKKEIVMPRQ IAMYLCRYLL SISLVSLANE
     FNRDHTTIMH GHDKIEAMIE EDQDFRQEIE ELIKEIKS
//
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