GenomeNet

Database: UniProt
Entry: A0A031FVR6_9MICO
LinkDB: A0A031FVR6_9MICO
Original site: A0A031FVR6_9MICO 
ID   A0A031FVR6_9MICO        Unreviewed;       474 AA.
AC   A0A031FVR6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-SEP-2017, entry version 28.
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   ECO:0000313|EMBL:EZP27685.1};
GN   ORFNames=BW34_01677 {ECO:0000313|EMBL:EZP27685.1};
OS   Microbacterium oleivorans.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=273677 {ECO:0000313|EMBL:EZP27685.1, ECO:0000313|Proteomes:UP000024001};
RN   [1] {ECO:0000313|EMBL:EZP27685.1, ECO:0000313|Proteomes:UP000024001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIT293 {ECO:0000313|EMBL:EZP27685.1,
RC   ECO:0000313|Proteomes:UP000024001};
RA   Gan H.Y., Gan H.M., Savka M.A., Hudson A.O.;
RT   "Draft Genome Sequences of 13 Willow Endophytes.";
RL   Submitted (MAR-2014) 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:EZP27685.1}.
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; JFYO01000005; EZP27685.1; -; Genomic_DNA.
DR   RefSeq; WP_036311236.1; NZ_JFYO01000005.1.
DR   EnsemblBacteria; EZP27685; EZP27685; BW34_01677.
DR   PATRIC; fig|273677.3.peg.1658; -.
DR   Proteomes; UP000024001; 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; 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:UP000024001};
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:UP000024001}.
FT   DOMAIN      167    295       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      379    448       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     175    182       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   474 AA;  52573 MW;  5982B001D7894292 CRC64;
     MSEHELPDVP VWSAVLDVLA QDDRVTPQLH GFVNLAVAQG VMSGTLYLDV PNDLTAGQFN
     KRLRGPIMEA LAQVDAEPAA STFRVVVNPE LGDAHLTAPV PVQSALAPTS SAPTRPGADD
     YAEQAAPASR NDTRLNPKYT FDSFVIGQSN RFAHAAAVAV AEAPAKAYNP LFIYGDSGLG
     KTHLLHAIGD YAINLYTGIK VRYVSSEEFT NDFINSIVNN RASAFQARYR DVDILLIDDI
     QFLQGRAETQ EAFFHTFNQL HDHDKQVVIT SDVPPRHLTG FEDRMRSRFE WGLITDVQAP
     DLETRIAILR KKAQSERLQV PDEVLEYIAT KVSSNIRELE GALIRVSAFA SLNRSNLDIS
     LAQTVLRDIV DQDDANVISP TDIISATAQY FRLTVDDLYG SSRSQSVATA RQIAMYLCRE
     RTSLSLPKIG QLFGNRDHTT VMYAYKKISE LMKERRSIYN QVSEITSQLG RSAR
//
DBGET integrated database retrieval system