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Database: UniProt
Entry: V9TWG1_9PROT
LinkDB: V9TWG1_9PROT
Original site: V9TWG1_9PROT 
ID   V9TWG1_9PROT            Unreviewed;       470 AA.
AC   V9TWG1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   05-JUL-2017, entry version 29.
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:AHC73660.1};
GN   ORFNames=P856_442 {ECO:0000313|EMBL:AHC73660.1};
OS   Candidatus Endolissoclinum faulkneri L5.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Candidatus Endolissoclinum.
OX   NCBI_TaxID=1401328 {ECO:0000313|EMBL:AHC73660.1, ECO:0000313|Proteomes:UP000018700};
RN   [1] {ECO:0000313|EMBL:AHC73660.1, ECO:0000313|Proteomes:UP000018700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L5 {ECO:0000313|EMBL:AHC73660.1};
RX   PubMed=24324632;
RA   Kwan J.C., Schmidt E.W.;
RT   "Bacterial endosymbiosis in a chordate host: long-term co-evolution
RT   and conservation of secondary metabolism.";
RL   PLoS ONE 8:E80822-E80822(2013).
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}.
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DR   EMBL; CP006745; AHC73660.1; -; Genomic_DNA.
DR   RefSeq; WP_025300539.1; NZ_CP006745.1.
DR   KEGG; efk:P856_442; -.
DR   PATRIC; fig|1401328.3.peg.431; -.
DR   KO; K02313; -.
DR   Proteomes; UP000018700; Chromosome.
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:UP000018700};
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:UP000018700}.
FT   DOMAIN      167    295       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      378    447       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     175    182       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   470 AA;  53539 MW;  A4F3E538C4F6AECA CRC64;
     MSELADCDEL AAQWARVKIR LRSECGETAY HAWLKSLTLA YRNGQIVYLV MPSKFERDRV
     VTQYGDRLRG LWQGEDPAIA AVEVVATSRR NNGLRPVDKL PKSNLAEEPI VNMLLMQEHI
     LSDPPGDFNA ISASLDDRFT FKNFVVGKPN ELAFAAAQRV AESDTIPFNP LFLYSGIGLG
     KTHLMCAMAW EIRKKYPQRR VIYLSAERFM YQFIRALRYR DTVTFKDLFR SVDVLMIDDV
     QFIGGKDSTQ EEFFHTFNAL VGNNRQVVIS ADKSPTNLDG LEERLRSRLG WGLVADIQPT
     DYELRLSILQ SKVKEVNVDI PTKVIEFLSH KISSNVRELE GALNRVVAHS TLVGLAITLE
     MVQEVLSDML QANNRQLTIE MIQRQVASHY KMDITDMYSA RRAQAIARPR QIAMYLAKNL
     TQHSLPEIGR KFGGRDHTTV MHAIKKVDEL RATNNSFDAD LTILRKMLEK
//
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