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Database: UniProt
Entry: A0A0F0ESE3_9MICO
LinkDB: A0A0F0ESE3_9MICO
Original site: A0A0F0ESE3_9MICO 
ID   A0A0F0ESE3_9MICO        Unreviewed;       555 AA.
AC   A0A0F0ESE3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   25-OCT-2017, entry version 20.
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=UB45_05970 {ECO:0000313|EMBL:KJK12848.1};
OS   Terrabacter sp. 28.
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Terrabacter.
OX   NCBI_TaxID=1619947 {ECO:0000313|EMBL:KJK12848.1, ECO:0000313|Proteomes:UP000033603};
RN   [1] {ECO:0000313|EMBL:KJK12848.1, ECO:0000313|Proteomes:UP000033603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=28 {ECO:0000313|EMBL:KJK12848.1,
RC   ECO:0000313|Proteomes:UP000033603};
RA   Roco C.A., Bergaust L., Bakken L., Yavitt J., Shapleigh J.P.;
RT   "The modularity of denitrifying soil bacteria: using gas kinetics and
RT   genome sequencing to connect denitrifier phenotype to genotype.";
RL   Submitted (FEB-2015) 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:KJK12848.1}.
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DR   EMBL; JYOE01000007; KJK12848.1; -; Genomic_DNA.
DR   RefSeq; WP_045189021.1; NZ_JYOE01000007.1.
DR   EnsemblBacteria; KJK12848; KJK12848; UB45_05970.
DR   PATRIC; fig|1619947.3.peg.4205; -.
DR   Proteomes; UP000033603; 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:UP000033603};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033603}.
FT   DOMAIN      248    382       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      460    529       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     256    263       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   555 AA;  61271 MW;  EE8FA12007E415D7 CRC64;
     MAETGVDYAR IWQQTLGTLD SGLSNQERAF VRLCRLVGVL DQIALVRAPN TFTKDFLETR
     VREQVHTALA DQLGHPVQVA VSVDESLETD LGMISDEPTG QVNDGRRQSG SDSNGSAGHH
     NGLAQGGAAT GSAGFGSPAH PGIHPQAHHA QHNPLRDLAE SAPALNGADL DEPARPAYPD
     VQTQMELGPD PLSGGESGPL RLQQRPEPSS PGDTRLNPKY TFDTFVIGAS NRFAHAAAVA
     VAEAPAKAYN PLFVYGESGL GKTHLLHAIG HYARTMFPNV RVRYVNSEEF TNDFINSIRD
     DKASAFQNRY RSVDVLLIDD IQFLQGKLQT QEEFFHTFNT LHNANKQIVI TSDLPPRELS
     GFEDRMRTRF ESGLLTDVQP PDLETRIAIL RKKAIQDRMS VPDDVLEYIA TNFSTNIREL
     EGALIRVTAF SNLNRQPVDL PLAEIVLKDV LPNETPNQVT AATIMAVTAA YYAVTIEDLC
     GSSRSRQLVT ARQIAMYLCR EMTDLSLPKI GQHFGGRDHT TVMHADRKIR ELMGERRAIY
     NQVTELTNRI RQQSH
//
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