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Database: UniProt
Entry: A0A117SJZ3_9FIRM
LinkDB: A0A117SJZ3_9FIRM
Original site: A0A117SJZ3_9FIRM 
ID   A0A117SJZ3_9FIRM        Unreviewed;       384 AA.
AC   A0A117SJZ3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   05-JUL-2017, entry version 9.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|RuleBase:RU000577};
GN   ORFNames=APF77_04200 {ECO:0000313|EMBL:KUO75605.1};
OS   Clostridia bacterium BRH_c25.
OC   Bacteria; Firmicutes; Clostridia.
OX   NCBI_TaxID=1734399 {ECO:0000313|EMBL:KUO75605.1, ECO:0000313|Proteomes:UP000057710};
RN   [1] {ECO:0000313|EMBL:KUO75605.1, ECO:0000313|Proteomes:UP000057710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c25 {ECO:0000313|EMBL:KUO75605.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-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|RuleBase:RU000577}.
CC   -!- SIMILARITY: Belongs to the DnaA family.
CC       {ECO:0000256|RuleBase:RU004227, 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:KUO75605.1}.
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DR   EMBL; LOES01000060; KUO75605.1; -; Genomic_DNA.
DR   Proteomes; UP000057710; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001957; Chromosome_initiator_DnaA.
DR   InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR   InterPro; IPR013317; DnaA.
DR   InterPro; IPR024633; DnaA_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR30050:SF12; PTHR30050:SF12; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF11638; DnaA_N; 1.
DR   PRINTS; PR00051; DNAA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU000577};
KW   Complete proteome {ECO:0000313|Proteomes:UP000057710};
KW   DNA replication {ECO:0000256|RuleBase:RU004227};
KW   DNA-binding {ECO:0000256|RuleBase:RU000577};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000577};
KW   Reference proteome {ECO:0000313|Proteomes:UP000057710}.
FT   DOMAIN      193    321       AAA. {ECO:0000259|SMART:SM00382}.
SQ   SEQUENCE   384 AA;  43945 MW;  9AE016C74907A30F CRC64;
     MEDMLSQILS DLNSLKEAVI EIDDRLKKLE CGGQIAEVGG MSEEKSGAGN RVFNTPAVEK
     PDYIWRKVLD IIKKELTEVS FKTWMEIVVP LSIDNDTIRL GVPGEFEKGI LECRYASLIK
     TALRSIINKD YKLEFSISGE KKKVISNKRI VVDTFEKRCS LNPKYSFDTL VIGEHNYLAY
     RYILDTVKNP DNHHGLAYIY GKVGIGKTHL IQAAGNYISE HYPAAKVLYI SIEAFTNAMI
     DAIRYDNSMG FKERMLSYDV LLIDDLQFIT GKEFTQAEFF KTVSEVLERG KQVVIACTGP
     PQDMTIMNER FTSMFELGGV FEIKRPDLDT RVEILRRIRA EENIKLSDEE LRTIAEKTFD
     NVRELLNAYN RYVTYAEMTG EKIK
//
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