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Database: UniProt
Entry: A0A0E4G9T1_9FIRM
LinkDB: A0A0E4G9T1_9FIRM
Original site: A0A0E4G9T1_9FIRM 
ID   A0A0E4G9T1_9FIRM        Unreviewed;       435 AA.
AC   A0A0E4G9T1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 27.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=848 {ECO:0000313|EMBL:CFX25011.1};
OS   Syntrophomonas zehnderi OL-4.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=690567 {ECO:0000313|EMBL:CFX25011.1, ECO:0000313|Proteomes:UP000045545};
RN   [1] {ECO:0000313|EMBL:CFX25011.1, ECO:0000313|Proteomes:UP000045545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OL-4 {ECO:0000313|EMBL:CFX25011.1,
RC   ECO:0000313|Proteomes:UP000045545};
RA   Murphy D.;
RL   Submitted (MAR-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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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; CGIH01000012; CFX25011.1; -; Genomic_DNA.
DR   RefSeq; WP_046496181.1; NZ_CGIH01000012.1.
DR   EnsemblBacteria; CFX25011; CFX25011; EBG00005169405.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000045545; 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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000045545};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000045545}.
FT   DOMAIN      127    255       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      339    408       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     135    142       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   435 AA;  49809 MW;  4E2C5A5BC37338CF CRC64;
     MSYDYDYIAV WDKVLQSVKA EIGSTSFDIW FPQVKYNTCR NEKIYISVPN TLTKEWIESR
     YLENMQKTFR DLTQQDINLI LTTEPIGKDA YISPLNPKYT FDTFVVGNSN RFAHAACYAV
     GEAPSRAYNP LFIYGGVGLG KTHLMQAIGH RILANNPKYS VMYVSSEQFT NELIGAIKDD
     NTPGFRNKYR NIDVLLIDDI QFLAGKERTQ EEFFHTFNTL YEANKQLVIS SDRPPRNIPT
     LEDRLRSRFE WGLITDIQIP DLETRIAILR KKAQTDDFNI PYDVLDYIAN YIDSNIRELE
     GALVRLVAYA TINDKPLNMA TAAEALKDIL PPPGPKKITI ECIQKEVCKY YDLELSEMLS
     KKRNKQLVVP RQIAMYICRK LTDASLPLIG DQFGGRDHTT VLHSLDKIDR EINEQPELAA
     VIDQLCKQVD PAYGS
//
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