GenomeNet

Database: UniProt
Entry: A0A0S2VZ72_9FIRM
LinkDB: A0A0S2VZ72_9FIRM
Original site: A0A0S2VZ72_9FIRM 
ID   A0A0S2VZ72_9FIRM        Unreviewed;       440 AA.
AC   A0A0S2VZ72;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   05-JUL-2017, entry version 14.
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   ORFNames=IB211_00001 {ECO:0000313|EMBL:ALP92397.1};
OS   Intestinimonas butyriciproducens.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Intestinimonas.
OX   NCBI_TaxID=1297617 {ECO:0000313|EMBL:ALP92397.1, ECO:0000313|Proteomes:UP000064844};
RN   [1] {ECO:0000313|Proteomes:UP000064844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF211 {ECO:0000313|Proteomes:UP000064844};
RA   de Vos W.M., Bui N.T.P., Plugge C.M., Ritari J.;
RT   "A butyrogenic pathway from the amino acid lysine in a human gut
RT   commensal.";
RL   Submitted (APR-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: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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP011307; ALP92397.1; -; Genomic_DNA.
DR   RefSeq; WP_058116688.1; NZ_CP011307.1.
DR   EnsemblBacteria; ALP92397; ALP92397; IB211_00001.
DR   KEGG; ibu:IB211_00001; -.
DR   PATRIC; fig|1297617.4.peg.1; -.
DR   KO; K02313; -.
DR   Proteomes; UP000064844; 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:UP000064844};
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:UP000064844}.
FT   DOMAIN      133    261       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      345    414       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     141    148       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   440 AA;  50525 MW;  5EAD37E5E35D20F9 CRC64;
     MNSAADIWSK VLSLMEADMT ATTIHTWFDD TVALSLDEDK FILHTPSDFK RDIILSRYLP
     PIQKALHELF SADFQVVVLG VEELEKYQNS RRPKEDGFLP GTEEYTFERF VVGSSNKFAH
     AAARAVADHP ALNYNPLFIY GESGLGKTHL LYAIAHKIHA DHPDYRIVYI KGDAFTNELI
     QAIREGRNQE FREKFRSADV FLMDDVQFIA GKDSTMEEMF HTFNTLYETR KQIVFTADRP
     PKEMLKLEDR LKTRFEWGLI ADIQPPDYET RMAIIKNKAI RMGVELPEAV LQYVAENITA
     NVRQIEGTVN KIMALRDLEG SNIDAATVTR AVRDMFKDPS DIMPTSDVII EEVCNFYNID
     NSALRGQGRT KDTALARQVA MYLIREMTNL SLKEIGREFE NRDHTTVLHS IERVEKLKKS
     TPEITEVIKD IRSNINARYE
//
DBGET integrated database retrieval system