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Database: UniProt
Entry: H5TDX2_9ALTE
LinkDB: H5TDX2_9ALTE
Original site: H5TDX2_9ALTE 
ID   H5TDX2_9ALTE            Unreviewed;       474 AA.
AC   H5TDX2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   05-JUL-2017, entry version 36.
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   ECO:0000313|EMBL:GAB56499.1};
GN   ORFNames=GPUN_2384 {ECO:0000313|EMBL:GAB56499.1};
OS   Glaciecola punicea ACAM 611.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Glaciecola.
OX   NCBI_TaxID=1121923 {ECO:0000313|EMBL:GAB56499.1, ECO:0000313|Proteomes:UP000053586};
RN   [1] {ECO:0000313|EMBL:GAB56499.1, ECO:0000313|Proteomes:UP000053586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB56499.1,
RC   ECO:0000313|Proteomes:UP000053586};
RX   PubMed=22628500; DOI=10.1128/JB.00463-12;
RA   Qin Q.-L., Xie B.-B., Shu Y.-L., Rong J.-C., Zhao D.-L., Zhang X.-Y.,
RA   Chen X.-L., Zhou B.-C., Zhanga Y.-Z.;
RT   "Genome sequence of proteorhodopsin-containing sea ice bacterium
RT   Glaciecola punicea ACAM 611T.";
RL   J. Bacteriol. 194:3267-3267(2012).
RN   [2] {ECO:0000313|EMBL:GAB56499.1, ECO:0000313|Proteomes:UP000053586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB56499.1,
RC   ECO:0000313|Proteomes:UP000053586};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals
RT   the high degree of genomic diversity and genomic characteristic for
RT   cold adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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:GAB56499.1}.
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DR   EMBL; BAET01000030; GAB56499.1; -; Genomic_DNA.
DR   RefSeq; WP_006006703.1; NZ_BAET01000030.1.
DR   EnsemblBacteria; GAB56499; GAB56499; GPUN_2384.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000053586; 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:UP000053586};
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:UP000053586}.
FT   DOMAIN      171    380       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      382    451       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     179    186       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   474 AA;  53917 MW;  5468C9753FB04A36 CRC64;
     MAISWKDCLE TLKHELETEQ FNMWLKPLVS YFDGETLFLY AANKFVLGWV RDEYFTLIMQ
     TLKQLYGADT PLLSIIDGKP PLVAEKSAPL ADKTSVSKTE NIVSPKLRIS DNINAGRRQS
     PSYSRSLPIP SLRNHNSNVN PKYTFDNFVE GKSNQLARAA ATQVSQNPGV TYNPLFLYGG
     TGLGKTHLIH AIGNGIVEKN PNAKIVYMHS ERFVQDMVKA LQNNAIEDFK RFYRSVDALL
     IDDIQLFANK DRSQEEFFHT FNALLEGNQQ IILTSDRYPK EIDGVEERLK SRFGWGLTVI
     IEPPELETRV AILLSKAKQN RIELPHEVAF FMAKKLRSNV RELEGALNRV IANANFTGKS
     ITIDFARDAL RDLLALQDKL VTIDNIIKTV AEYYKIKVAD VLSKRRTRSI ARPRQMAMAL
     AKELTNNSYP EIGNSFSGRD HTTVMHAVKK IKQLRAEDHD IMEDYTNLIR TLSY
//
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