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Database: UniProt
Entry: D9QS97_ACEAZ
LinkDB: D9QS97_ACEAZ
Original site: D9QS97_ACEAZ 
ID   D9QS97_ACEAZ            Unreviewed;       449 AA.
AC   D9QS97;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-SEP-2017, entry version 50.
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   OrderedLocusNames=Acear_0001 {ECO:0000313|EMBL:ADL11553.1};
OS   Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC   Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Acetohalobium.
OX   NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL11553.1, ECO:0000313|Proteomes:UP000001661};
RN   [1] {ECO:0000313|EMBL:ADL11553.1, ECO:0000313|Proteomes:UP000001661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC   {ECO:0000313|Proteomes:UP000001661};
RX   PubMed=21304692;
RA   Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C.,
RA   Brambilla E., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Bruce D., Detter C., Tapia R., Goodwin L.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Rohde M., Goker M., Spring S., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT   7288).";
RL   Stand. Genomic Sci. 3:57-65(2010).
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}.
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DR   EMBL; CP002105; ADL11553.1; -; Genomic_DNA.
DR   RefSeq; WP_013277000.1; NC_014378.1.
DR   STRING; 574087.Acear_0001; -.
DR   EnsemblBacteria; ADL11553; ADL11553; Acear_0001.
DR   KEGG; aar:Acear_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000001661; 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; 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:UP000001661};
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:UP000001661}.
FT   DOMAIN      145    273       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      357    426       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     153    160       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   449 AA;  51898 MW;  2418EF783AC6AADF CRC64;
     MKKEDLTEIW QEALEIFKSE LSKPSFKTWL KSTKLISVEN DHAVIEVPNE FSKDWLETRY
     SNLIKETISQ LIDRKINIKF TIPTNKEEKL VNKKKKDKKT DNQEEDDNNP ASLNPKYTFD
     TFVIGSSNRF AHAASLAVAE APAKAYNPLF IYGDVGLGKT HLMHAIGHYI IEHNSDLKVV
     YVTSEKFTNE LINSIRDDNT VKFRNKYRNI DILLIDDIQF LAGKERTQEE FFHTFNALHE
     ANKQIIISSD RPPKEIPTLE ERLRSRFEWG LITDIQEPDL ETRIAILRKK ATLEDLEVPN
     EVIVYIANQI HSNIRELEGA LIRVVAYSSL TNKEITVELA QEALKDIIST TEAEEINIKL
     IQQIVANHYN LEIEDMKSRK RTRAIAFPRQ VAMYLSRELT DSSLPKIGEK FGGRDHTTVL
     HAYNKIDDKK EEDIQFKNTI KTLTNKINN
//
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