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Database: UniProt
Entry: U7D9S5_9BACT
LinkDB: U7D9S5_9BACT
Original site: U7D9S5_9BACT 
ID   U7D9S5_9BACT            Unreviewed;       462 AA.
AC   U7D9S5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   05-JUL-2017, entry version 29.
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=CALK_1974 {ECO:0000313|EMBL:ERP31175.1};
OS   Chitinivibrio alkaliphilus ACht1.
OC   Bacteria; Fibrobacteres; Chitinivibrionia; Chitinivibrionales;
OC   Chitinivibrionaceae; Chitinivibrio.
OX   NCBI_TaxID=1313304 {ECO:0000313|EMBL:ERP31175.1, ECO:0000313|Proteomes:UP000017148};
RN   [1] {ECO:0000313|EMBL:ERP31175.1, ECO:0000313|Proteomes:UP000017148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACht1 {ECO:0000313|EMBL:ERP31175.1,
RC   ECO:0000313|Proteomes:UP000017148};
RX   PubMed=24112708;
RA   Sorokin D.Y., Gumerov V.M., Rakitin A.L., Beletsky A.V., Damste J.S.,
RA   Muyzer G., Mardanov A.V., Ravin N.V.;
RT   "Genome analysis of Chitinivibrio alkaliphilus gen. nov., sp. nov., a
RT   novel extremely haloalkaliphilic anaerobic chitinolytic bacterium from
RT   the candidate phylum Termite Group 3.";
RL   Environ. Microbiol. 0:0-0(2013).
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:ERP31175.1}.
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DR   EMBL; ASJR01000018; ERP31175.1; -; Genomic_DNA.
DR   RefSeq; WP_022637394.1; NZ_ASJR01000018.1.
DR   EnsemblBacteria; ERP31175; ERP31175; CALK_1974.
DR   PATRIC; fig|1313304.3.peg.1880; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000017148; Unassembled WGS sequence.
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:UP000017148};
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:UP000017148}.
FT   DOMAIN      159    295       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      369    438       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     167    174       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   462 AA;  52028 MW;  20E10339C15731AE CRC64;
     MDKNILWTKT LARLKEDLSV REISYTNWLE PLHPLSYAQG VLLLKTDNPF GLEVLNTQYR
     KIVLHHAQQI DPNIEALGFT IEENAAPPRA EELQPDHAAT NRVDSQKKHS KKDRKKKEWN
     KKGLPINTKL TFASFIEAEE TDLAYHSAKA VAENPGARRF NPLFIYGECG VGKTHLLHAM
     ANTIQQERPN LRIVFTSAKE FYHDFFSSLN EKTMDEFKKH YTTCDVLFMD DIHTLSGKES
     SQTEVFKIFN DLHTQNRQMV FAAPCPPEAL SGIADRLLTR LQWGLSVHID APQLETRSAI
     LRTLLENESV QISHEAIHYL AQKGPRSIGD LEGISVRVAA HYSLGNKPIN STTAAEILYN
     DGITPGKIRA IDIITAITDE FGISRQLLTS KSRSKEVAQA RQIGMFLCKE HTDLSLKAIG
     TEFGGRDHST VVHAVKTVGA KMEQDTPFAQ RVDTIIRRAR QA
//
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