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Database: UniProt
Entry: A0A0G1GTL6_9BACT
LinkDB: A0A0G1GTL6_9BACT
Original site: A0A0G1GTL6_9BACT 
ID   A0A0G1GTL6_9BACT        Unreviewed;       488 AA.
AC   A0A0G1GTL6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   25-OCT-2017, entry version 17.
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   ORFNames=UW27_C0007G0010 {ECO:0000313|EMBL:KKT37955.1};
OS   Parcubacteria group bacterium GW2011_GWA1_44_13.
OC   Bacteria; unclassified Parcubacteria group.
OX   NCBI_TaxID=1618788 {ECO:0000313|EMBL:KKT37955.1, ECO:0000313|Proteomes:UP000034180};
RN   [1] {ECO:0000313|EMBL:KKT37955.1, ECO:0000313|Proteomes:UP000034180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT   large radiation of phyla.";
RL   Nature 0:0-0(2015).
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: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:KKT37955.1}.
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DR   EMBL; LCHR01000007; KKT37955.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKT37955; KKT37955; UW27_C0007G0010.
DR   PATRIC; fig|1618788.3.peg.404; -.
DR   Proteomes; UP000034180; 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; IPR024633; DnaA_N_dom.
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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034180};
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:UP000034180}.
FT   DOMAIN      186    320       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      398    467       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     194    201       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   488 AA;  56409 MW;  CFD2813142D41B90 CRC64;
     MNFHSLSTPY SPTHPPTLFH YLFHKEYNVE TNPNNLMINN AQLWEKTLFE LEGELSRANF
     STWFKNTAIL KQDDGVVIVG VPNEFVKDWL QNKFHKTILR SLRNLSENIR GIEYAVCKIE
     EPKIEKKSVD QIKTAQGAEL PLNDLYINKE DGLNPRYTFN DFIIGAFNEL AYAASQAILK
     KVGTNVYNPL FIYGNTGLGK THLIQAIGNQ VKSHYPNKRV FYTTSEKFSV DYINSVGQGA
     KAMAVFKNKY RVYDLLIMDD IQFLSNKEKT QEELFHIFNE LYHNNKQIIF SSDKHPNYIP
     ALEARLKSRF SAGMIVDIQE PEYESRLAIL RAKAETQKFF PPEEIIEYLA SSVNGNIREL
     EGLLNGIICQ SELKNRNLTL NEIKPFIKNS AKPKKLLSVK EIVKVVCDFY SIEESFVYEK
     TRRKEILKPR QIAMFILRED FNISYPTIGQ KLGGRDHTTV MHSCEKVKID IKNDLSLMQE
     VDQIRAMF
//
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