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Database: UniProt
Entry: A0A0M2RHD3_9ACTN
LinkDB: A0A0M2RHD3_9ACTN
Original site: A0A0M2RHD3_9ACTN 
ID   A0A0M2RHD3_9ACTN        Unreviewed;       604 AA.
AC   A0A0M2RHD3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   25-OCT-2017, entry version 17.
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=LQ51_26365 {ECO:0000313|EMBL:KKJ95758.1};
OS   Micromonospora sp. HK10.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Micromonospora.
OX   NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKJ95758.1, ECO:0000313|Proteomes:UP000034330};
RN   [1] {ECO:0000313|EMBL:KKJ95758.1, ECO:0000313|Proteomes:UP000034330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK10 {ECO:0000313|EMBL:KKJ95758.1,
RC   ECO:0000313|Proteomes:UP000034330};
RA   Talukdar M., Das D., Borah C., Deka Boruah H.P., Bora T.C.,
RA   Singh A.K.;
RT   "Draft genome sequence of Micromonospora HK10, isolated from Kaziranga
RT   National park, Assam, India.";
RL   Submitted (NOV-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:SAAS00735475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
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:KKJ95758.1}.
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DR   EMBL; JTGL01000206; KKJ95758.1; -; Genomic_DNA.
DR   RefSeq; WP_046563064.1; NZ_KQ058674.1.
DR   EnsemblBacteria; KKJ95758; KKJ95758; LQ51_26365.
DR   PATRIC; fig|1538294.3.peg.607; -.
DR   Proteomes; UP000034330; 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:SF2; PTHR30050:SF2; 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:SAAS00747950};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034330};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895}.
FT   DOMAIN      298    426       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      510    579       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     306    313       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      579    604       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   604 AA;  66466 MW;  49A9F685ED6922BC CRC64;
     MTGATDLAAV WTATTDELAD EIISAQQRAY LRLTRLRAIV EDTALLSVPD AFTRDVIESR
     LRPAITEALS RRLGRPIQVA VTVRVAEDGR PAGTVYRSGP EPAELDAPQD LLAGFDQPGP
     PSEPPGFPEF GFPARTDSAG YPEPRAEQPA EESAPRQRAP EANRPPLIPA SRDGQETLFS
     AAFGDPMRGA PERRGFEDRA VDTPAADGRG FEPRYRENPA AAPPLRGLPG SGATDSGPGR
     GGTDHRPGGS ADRRLPGGAE SGGNRLNPKY MFETFVIGSS NRFAHAASVA VAESPAKAYN
     PLFIYGSSGL GKTHLLHAIG HYATTLGNAR SVRYVSTEEF TNDFINSLRD DKTSAFQRRY
     RDVDILLIDD IQFLENRERT QEEFFHTFNT LHNANKQIVI TSDRSPKQLA TLEDRLRTRF
     EWGLLADIQP PDLETRIAIL QKKAAQERLF APPDVLEFIA SRVSNSIREL EGALIRVTAF
     ASLTRSSVEL SLAEEVLRDF IPDGAGPEIT ADQIMVSTAD YFGVSLEDLR GHSRSRVLVN
     ARQVAMYLCR ELTDLSLPRI GQAFGGRDHT TVMHADRKIR QQMAERRSLY NQIAELTNRI
     KQTT
//
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