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Database: UniProt
Entry: A0A140DR58_9FIRM
LinkDB: A0A140DR58_9FIRM
Original site: A0A140DR58_9FIRM 
ID   A0A140DR58_9FIRM        Unreviewed;       425 AA.
AC   A0A140DR58;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   25-OCT-2017, entry version 13.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=AALO17_00010 {ECO:0000313|EMBL:AMK53135.1};
OS   Faecalibaculum rodentium.
OC   Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Faecalibaculum.
OX   NCBI_TaxID=1702221 {ECO:0000313|EMBL:AMK53135.1, ECO:0000313|Proteomes:UP000069771};
RN   [1] {ECO:0000313|EMBL:AMK53135.1, ECO:0000313|Proteomes:UP000069771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alo17 {ECO:0000313|EMBL:AMK53135.1,
RC   ECO:0000313|Proteomes:UP000069771};
RX   PubMed=26877770; DOI=10.1186/s13099-016-0087-3;
RA   Lim S., Chang D.H., Ahn S., Kim B.C.;
RT   "Whole genome sequencing of "Faecalibaculum rodentium" ALO17, isolated
RT   from C57BL/6J laboratory mouse feces.";
RL   Gut Pathog 8:3-3(2016).
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:SAAS00747914}.
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}.
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DR   EMBL; CP011391; AMK53135.1; -; Genomic_DNA.
DR   EnsemblBacteria; AMK53135; AMK53135; AALO17_00010.
DR   KEGG; fro:AALO17_00010; -.
DR   PATRIC; fig|1702221.3.peg.1; -.
DR   KO; K02313; -.
DR   Proteomes; UP000069771; Chromosome.
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; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
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   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.
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:UP000069771};
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:UP000069771}.
FT   DOMAIN      120    253       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      334    403       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     128    135       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   425 AA;  48164 MW;  48A4EE6B7C74076F CRC64;
     MTCRDWISRT RLIYLDPQTA RVYCPSRITQ SILRQEQALF ETLLCEQTGT PVSLQLTDRV
     EQQTEPAPSF PSTPPATPSV PLLQARFNPE YTFDSFVEGT SNKEAYAAVY NSCIQTGIRA
     FNPIMIYGNS GLGKTHLLHA AGNWLRLNRP EDKVIYMDAN TFVDLLIEAM KSKTVDSVKS
     RLTDCDFFLL DDIQNLRRSS SQEIFFTVYN ELISQNTQVM MTSDIHPQDL SGLQARLISR
     FTSGLTVSIS RPEFDTSRAI LRKRIEGKEE QIRIQDDVID YLASTFSNDV RNLEGSLNRL
     IFSATLENPE VIDTAFAKAV LVNEPIVDRQ KELTLHKIEK AVTNFYGLTC SDLEGKSRQK
     AIVNARHICV YLARELLHTS YSQIGQQLGG RDHKTIASSY ERAEKLIRQD QAFSLAVTRI
     QESLQ
//
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