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Database: UniProt
Entry: K2Q3G4_9FLAO
LinkDB: K2Q3G4_9FLAO
Original site: K2Q3G4_9FLAO 
ID   K2Q3G4_9FLAO            Unreviewed;       475 AA.
AC   K2Q3G4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   16-JAN-2019, entry version 43.
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   ECO:0000313|EMBL:EKF55391.1};
GN   ORFNames=I215_07991 {ECO:0000313|EMBL:EKF55391.1};
OS   Galbibacter marinus.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Galbibacter.
OX   NCBI_TaxID=555500 {ECO:0000313|EMBL:EKF55391.1, ECO:0000313|Proteomes:UP000007364};
RN   [1] {ECO:0000313|EMBL:EKF55391.1, ECO:0000313|Proteomes:UP000007364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ck-I2-15 {ECO:0000313|Proteomes:UP000007364};
RX   PubMed=23209227; DOI=10.1128/JB.01852-12;
RA   Lai Q., Li C., Shao Z.;
RT   "Genome Sequence of Galbibacter marinum Type Strain ck-I2-15.";
RL   J. Bacteriol. 194:6973-6973(2012).
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:EKF55391.1}.
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DR   EMBL; AMSG01000008; EKF55391.1; -; Genomic_DNA.
DR   RefSeq; WP_008991453.1; NZ_AMSG01000008.1.
DR   EnsemblBacteria; EKF55391; EKF55391; I215_07991.
DR   PATRIC; fig|555500.3.peg.1656; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000007364; 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:UP000007364};
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:UP000007364}.
FT   DOMAIN      172    308       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      383    452       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     180    187       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   475 AA;  54564 MW;  A725BBD2801E016A CRC64;
     MNVTAESVWE NCLHFIKDNI QPQAFKTWFE PIKSVKLTDK ALSIQVPSKF FYEWLEEHYV
     KLLKVALTRE LGENAKLVYV IRMENTYGNK QPFTESIPSS NRANMQPQEL DVPVKHKNPE
     LKNPFVIPGI RNIKIESQLN PNYSFDNFLE GDSNRLARSA GMAVANKPGG TSFNPLLIFG
     GVGLGKTHLA HAIGVEIKDK YPEKTVLYIS AEKFTQQYIE SVKKNTRNDF IHFYQLIDVL
     IIDDVQFFSG KSGTQDVFFH VFNHLHQNGK QVILTSDKAP VDMQDIEQRL LSRFKWGLSA
     ELQNPDYETR VSILKNRLYR DGVEMPEEII DCVARNIKSN VRELEGAIIS LIAQSSFNKK
     EVTLELANQI VEKFVKNTKR EVSIDYIQKV ISDYFQMDVE TLQSKTRKRH IVQARQLAMF
     FAKKYTKASL ASIGSQIGKR DHATVLHACK TVDNLAETDK QFRKYIDDLN QKFSQ
//
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