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Database: UniProt
Entry: S6A7Q6_9SPIO
LinkDB: S6A7Q6_9SPIO
Original site: S6A7Q6_9SPIO 
ID   S6A7Q6_9SPIO            Unreviewed;       462 AA.
AC   S6A7Q6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   05-JUL-2017, entry version 31.
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:AGT42504.1};
GN   ORFNames=TPE_0001 {ECO:0000313|EMBL:AGT42504.1};
OS   Treponema pedis str. T A4.
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=1291379 {ECO:0000313|EMBL:AGT42504.1, ECO:0000313|Proteomes:UP000015620};
RN   [1] {ECO:0000313|EMBL:AGT42504.1, ECO:0000313|Proteomes:UP000015620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T A4 {ECO:0000313|EMBL:AGT42504.1};
RX   PubMed=23977007; DOI=10.1371/journal.pone.0071281;
RA   Svartstrom O., Mushtaq M., Pringle M., Segerman B.;
RT   "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic
RT   Skin Lesions of Pigs, with the Human Oral Pathogen Treponema
RT   denticola.";
RL   PLoS ONE 8:E71281-E71281(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; CP004120; AGT42504.1; -; Genomic_DNA.
DR   RefSeq; WP_020963804.1; NC_022097.1.
DR   EnsemblBacteria; AGT42504; AGT42504; TPE_0001.
DR   KEGG; tped:TPE_0001; -.
DR   PATRIC; fig|1291379.3.peg.1; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000015620; 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:UP000015620};
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:UP000015620}.
FT   DOMAIN      155    286       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      366    435       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     163    170       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   462 AA;  52974 MW;  AACF8897A8D877F1 CRC64;
     MSEWNYELFW DEIISQFKNE LQEASFSMFF AVIRYKASTK TSIIIEVPSQ FIKIQIMQRY
     QADIERKLLE ISGQKLLVEF EVSTVPITNS QNEPEEDTHS LNTKTIVKPA PKKNESRGAH
     PSLNEDYNFD DFIVGPNNNF AVNAALAITK NPGTSYNPFL IYGGVGLGKT HLMQAIGNDI
     WKNTKLKVIY VTAENFTNEF VECVQKKAMP SFKSKYRTAD ILLIDDIHFF QGKAETQEEL
     FHTFNELYER NKQIVFTCDR PPSELKNLSK RLQSRFERGL NVDLQTPGFE TRCAILLKKL
     EKRSVKIPEK VVQMVAKNVS SNVRDLEAAL TKLIAYAELT KKEITEALAQ NLLRDFFGST
     RQRNVSVDII QKTVADYFRI SISDIKGKKR TKSFAYPRQI AMYLCRKMTE CSTTELGNEF
     GGRDHTTILH GCNKVEDLMR ADPGTEATIH ELQKQIKENI NK
//
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