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Database: UniProt
Entry: A0A0M9CCG1_9ACTN
LinkDB: A0A0M9CCG1_9ACTN
Original site: A0A0M9CCG1_9ACTN 
ID   A0A0M9CCG1_9ACTN        Unreviewed;       518 AA.
AC   A0A0M9CCG1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-SEP-2017, entry version 16.
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   ORFNames=ISGA_09250 {ECO:0000313|EMBL:KOY49613.1};
OS   Gordonia sp. NB4-1Y.
OC   Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia.
OX   NCBI_TaxID=1241906 {ECO:0000313|EMBL:KOY49613.1, ECO:0000313|Proteomes:UP000011989};
RN   [1] {ECO:0000313|EMBL:KOY49613.1, ECO:0000313|Proteomes:UP000011989}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB4-1Y {ECO:0000313|EMBL:KOY49613.1,
RC   ECO:0000313|Proteomes:UP000011989};
RX   PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA   Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT   "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in
RT   relation to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL   Microbiology 159:1618-1628(2013).
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:SAAS00731907}.
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:KOY49613.1}.
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DR   EMBL; APHK02000061; KOY49613.1; -; Genomic_DNA.
DR   RefSeq; WP_053777277.1; NZ_APHK02000061.1.
DR   EnsemblBacteria; KOY49613; KOY49613; ISGA_09250.
DR   Proteomes; UP000011989; 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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011989};
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:UP000011989}.
FT   DOMAIN      211    339       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      423    491       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     219    226       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   518 AA;  57155 MW;  D43BFFE69645C031 CRC64;
     MTSDRDSFGE VWQRVVAELN DDSAQGDHEP LTRQQKAWLS LVQPLTLAEG FALLTVPTPL
     VQEQIERNLR DTIRTTLSRH LGQPVDLGVR TATPPPVEEH TPADTPAPAA QSPAAAPGSQ
     VPASTAVPAA GSDGVGDHVP PARPAADGVV GPAPAGADWS SYFAERPATP TPAASPASLN
     PKYTFDTFVI GASNRFAHAS AVAVAEAPAR AYNPLFIWGE SGLGKTHLLH AAGHYAQRLF
     PGMRVKYVST EEFTNDFINS LRDDRRVAFK RRYRDVDVLL VDDIQFLIGK EGIQEEFFHT
     FNTLHNTSKQ IVISSDRPPK QLATLEDRLR TRFEWGLITD VQPPDLETRI AILRKKAQMD
     NIAVPDDVLE LIASKIERNI RELEGALIRV TAFASLNNTE LDKSLADVVL QALLPNDGTL
     EISAASILAI TAEYFDISVD ELRGPGKARS LAQARQISMY LCRELTDLSL PKIGETFDRD
     HTTVMYAERK IRKEMAERRK VYDHVQELTA RIKQRADR
//
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