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Database: UniProt
Entry: A0A0Q9MCI1_9MICO
LinkDB: A0A0Q9MCI1_9MICO
Original site: A0A0Q9MCI1_9MICO 
ID   A0A0Q9MCI1_9MICO        Unreviewed;       505 AA.
AC   A0A0Q9MCI1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   05-JUL-2017, entry version 15.
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=ASG78_01330 {ECO:0000313|EMBL:KRE63569.1};
OS   Tetrasphaera sp. Soil756.
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Tetrasphaera.
OX   NCBI_TaxID=1736399 {ECO:0000313|EMBL:KRE63569.1, ECO:0000313|Proteomes:UP000051616};
RN   [1] {ECO:0000313|EMBL:KRE63569.1, ECO:0000313|Proteomes:UP000051616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil756 {ECO:0000313|EMBL:KRE63569.1,
RC   ECO:0000313|Proteomes:UP000051616};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE63569.1, ECO:0000313|Proteomes:UP000051616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil756 {ECO:0000313|EMBL:KRE63569.1,
RC   ECO:0000313|Proteomes:UP000051616};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRE63569.1}.
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DR   EMBL; LMSE01000001; KRE63569.1; -; Genomic_DNA.
DR   EnsemblBacteria; KRE63569; KRE63569; ASG78_01330.
DR   Proteomes; UP000051616; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051616};
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:UP000051616}.
FT   DOMAIN      198    328       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      410    479       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     206    213       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      472    499       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   505 AA;  56530 MW;  8DFE8F204F840EBB CRC64;
     MMTELWSATL EALDDDGIPV QQRAFLGLAR LVGLLDDTAL IAVPNDFTKD QVETRLRDRV
     THTLSERLGR EVRLAVTVDP SLADLPADGQ EPEANGAGPQ DPDTDPGHDQ RAADRRQQIH
     DLALIDDDES GAGRDHHGRP ALVEVPGMRR PRPGTQVPEQ VELTRLNPKY TFDTFVIGAS
     NRFAHAAAVA VAEAPAKAYN PLFVYGDSGL GKTHLLHAIG HYARALFPNV KVRYVNSEEF
     TNDFINSIRD DKAANFQRRY RDVDVLLIDD IQFLQGKVQT QEEFFHTFNT LHNASKQVVI
     TSDVPPKLLT GFEARMRSRF EMGLLTDVQP PDLETRIAIL RKKAIQERLS VPDDVHEFIA
     SRISTNIREL EGALIRVTAF ASLNRQPVDM SLAEIVLRDL IPDDSTSQVT PATIIAQTAA
     YFGLTIEDLQ GQSRSRVLVT ARQIAMYLCR ELTDLSLPKI GQQFGGRDHT TVMHAEKKIR
     QLMAERRAIY NQVTELTNRI KQQSR
//
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