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Database: UniProt
Entry: K9EDZ1_9ACTO
LinkDB: K9EDZ1_9ACTO
Original site: K9EDZ1_9ACTO 
ID   K9EDZ1_9ACTO            Unreviewed;       590 AA.
AC   K9EDZ1;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   05-JUL-2017, entry version 34.
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=HMPREF9233_00779 {ECO:0000313|EMBL:EKU95414.1};
OS   Actinobaculum massiliense ACS-171-V-Col2.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC   Actinobaculum.
OX   NCBI_TaxID=883066 {ECO:0000313|EMBL:EKU95414.1, ECO:0000313|Proteomes:UP000009888};
RN   [1] {ECO:0000313|EMBL:EKU95414.1, ECO:0000313|Proteomes:UP000009888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-171-V-Col2 {ECO:0000313|Proteomes:UP000009888};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Saerens B.,
RA   Vaneechoutte M., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Actinobaculum massiliae ACS-171-V-COL2.";
RL   Submitted (SEP-2012) 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:SAAS00731907}.
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:EKU95414.1}.
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DR   EMBL; AGWL01000003; EKU95414.1; -; Genomic_DNA.
DR   RefSeq; WP_007000985.1; NZ_JH992955.1.
DR   EnsemblBacteria; EKU95414; EKU95414; HMPREF9233_00779.
DR   PATRIC; fig|883066.3.peg.807; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000009888; 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; 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   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:UP000009888};
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:UP000009888}.
FT   DOMAIN      279    413       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      491    560       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     287    294       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   590 AA;  64445 MW;  FD4148E515AB8968 CRC64;
     MSDSNPAQDA WLAAMELLRA EDTLSDSQAA FVRMAHPLAT ADDIFMVTVG SDFVKNWIEE
     HVSAQMAEKL SAILARSIRI VISVDPSINE TNLSSSPSEP APARQNATPV DQAAEVPGHQ
     TPETPHAVPT APAQGENPGS ASGEPARHGG REGEESTSWD GSSQWSSGSE ATSYVDLIAA
     RGHLDRGYQQ QAAPAQSSQR FRYGNSSTGN ATVEAARDAS AAASYTRTTP EEADDPTFAA
     RSHKAGLNPK YTFDNFVIGD SNRFPTATSL AVAESPGTSY NPLFLYSDSG MGKTHLMHAI
     GNYALALYPE INVRYVSAEE FTNAFINAVR DARQSEFKDF FRNVDILLID DIQFIGGRES
     TVEEFFHTFN ALTNQNKQIV ITSDVAPNLL NGFGERMLSR FNSGVVASID RPNLETRVAI
     LEKKSHADGI NVPRDVQEYI ATNMTTNVRE MEGALRRVTA YADLSKQPVS LSLAEMVLKD
     LISDPESVEI QPSVIMAHTA NYFRVTIEDL TSSDRSRLPT TARQIAMYLC REMTDLSLPK
     IGAIFGGRDH TTVMHAYRKI DKQMAERQTT YNQVSELSVR IKQDATGNGS
//
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