GenomeNet

Database: UniProt
Entry: A0A117KXC1_9FIRM
LinkDB: A0A117KXC1_9FIRM
Original site: A0A117KXC1_9FIRM 
ID   A0A117KXC1_9FIRM        Unreviewed;       446 AA.
AC   A0A117KXC1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-SEP-2017, entry version 12.
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=XD50_0344 {ECO:0000313|EMBL:KUK11303.1};
OS   Clostridia bacterium 41_269.
OC   Bacteria; Firmicutes; Clostridia.
OX   NCBI_TaxID=1635275 {ECO:0000313|EMBL:KUK11303.1, ECO:0000313|Proteomes:UP000053409};
RN   [1] {ECO:0000313|EMBL:KUK11303.1, ECO:0000313|Proteomes:UP000053409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=41_269 {ECO:0000313|EMBL:KUK11303.1};
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-resolved metagenomic analysis reveals roles for candidate
RT   phyla and other microbial community members in biogeochemical
RT   transformations in oil reservoirs.";
RL   MBio 7:e01669-15(2015).
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   -!- 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:KUK11303.1}.
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; LGEZ01000003; KUK11303.1; -; Genomic_DNA.
DR   PATRIC; fig|1635275.3.peg.1491; -.
DR   Proteomes; UP000053409; 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   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:UP000053409};
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:UP000053409}.
FT   DOMAIN      139    267       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      351    420       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     147    154       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   446 AA;  51122 MW;  3208580CF2C8C5E5 CRC64;
     MSLSLETLWK LALDILKREI NRTSFETWLK PTQLLSLENN RAVIFVPNEF AKEWLEARYY
     NLIQSTLEKI LKEEVHIIFT TLQKPGNFSL PKSSLTLEAK GITSAHLNPK YTFDTFVIGN
     SNRFAHAACL AVAEAPAHAY NPLFIYGGVG LGKTHLMHAI GHHVITNISN YRVLYVSSEK
     FTNELIDSIR DDKTTEFRDR YRNIDVLLID DIQFLAGKER TQEEFFHTFN TLYEANKQII
     ISSDRPPKEI PTLEDRLRSR FEWGLITDIQ PPDYETRLAI LKKKAELEKI VLPDEVMEYI
     ADNIHTNIRK LEGALLKVAA YASITNEEID VEFAAKILQD IIPKRKPVPI TIDLIQEKVA
     EYFKINVSEL KSKKRNRSVA FPRQIAMYLS RELTDASLPT IGSKFGGRDH TTVIHACDKI
     AKEVLKNPSL KEEIDHLKDQ ITKLSS
//
DBGET integrated database retrieval system