GenomeNet

Database: UniProt
Entry: V4PJX0_9CAUL
LinkDB: V4PJX0_9CAUL
Original site: V4PJX0_9CAUL 
ID   V4PJX0_9CAUL            Unreviewed;       451 AA.
AC   V4PJX0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   23-MAY-2018, entry version 35.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01020005};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=AEAC466_00660 {ECO:0000313|EMBL:ESQ85715.1};
OS   Asticcacaulis sp. AC466.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ85715.1, ECO:0000313|Proteomes:UP000017826};
RN   [1] {ECO:0000313|EMBL:ESQ85715.1, ECO:0000313|Proteomes:UP000017826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC466 {ECO:0000313|EMBL:ESQ85715.1,
RC   ECO:0000313|Proteomes:UP000017826};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00747961}.
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:ESQ85715.1}.
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DR   EMBL; AWGE01000001; ESQ85715.1; -; Genomic_DNA.
DR   EnsemblBacteria; ESQ85715; ESQ85715; AEAC466_00660.
DR   PATRIC; fig|1282362.3.peg.131; -.
DR   Proteomes; UP000017826; 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:UP000017826};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00747973};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00748008};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017826}.
FT   DOMAIN      139    267       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      358    427       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     147    154       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   451 AA;  50078 MW;  9673F1DA733F8AAF CRC64;
     MGEGPFNSYV APSSVRPGPY GDPVLVTPTA YARDWIARNA ARRAQELWTQ HDPDSRVLEI
     KSRVEYEDQT RQAPLAGAAE TPVVDAPAPA APQMPIVEIA ANRISGLQER LTFESFVSGR
     GNEFAYTMSR QVASWADGHF NPVFFHGPYG YGKTHLLNAI GWEAQSRRPD ARIVYLTAEK
     FTSTFVKALM DKSTAAFKDE VRGADLLLVD DVHFIGGKTS SQEELFHTLT SLIENNRRVV
     FTADRPPSQL TEIEARLRSH LSSGLVCALD VADQSLRMGI IERKLEQLSQ RIGSSGQAPR
     ADVLHFLAER VPGSIRELEG AVNTLVASAG PRLGSLTLEE AMALLQPNLK VAVERRVTVD
     EIQKLTADHF GLKQADLLSE RRTRSVARPR QVAMWLCKQH TTRSYPDIGR RFGGRDHTTV
     LHAVKKVEEL LQADDQIARD VEALTRKLRN T
//
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