GenomeNet

Database: UniProt
Entry: A0A161MKK3_9MICO
LinkDB: A0A161MKK3_9MICO
Original site: A0A161MKK3_9MICO 
ID   A0A161MKK3_9MICO        Unreviewed;       464 AA.
AC   A0A161MKK3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   25-OCT-2017, entry version 14.
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:GAT74733.1};
GN   ORFNames=MHM582_3241 {ECO:0000313|EMBL:GAT74733.1};
OS   Microbacterium sp. HM58-2.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1778770 {ECO:0000313|EMBL:GAT74733.1, ECO:0000313|Proteomes:UP000077073};
RN   [1] {ECO:0000313|Proteomes:UP000077073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HM58-2 {ECO:0000313|Proteomes:UP000077073};
RG   Microbacterium sp. strain HM58-2 genome sequencing;
RA   Akiyama T., Ishige T., Kanesaki Y., Ito S., Oinumam K., Takaya N.,
RA   Sasaki Y., Yajima S.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000077073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HM58-2 {ECO:0000313|Proteomes:UP000077073};
RA   Akiyama T., Ishige T., Kanesaki Y., Ito S., Oinumam K., Takaya N.,
RA   Sasaki Y., Yajima S.;
RT   "Draft genome sequence of Microbacterium sp. strain HM58-2 that
RT   catabolites acylhydrazides.";
RL   Submitted (MAY-2016) 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:GAT74733.1}.
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; BDCY01000005; GAT74733.1; -; Genomic_DNA.
DR   RefSeq; WP_067357042.1; NZ_BDCY01000005.1.
DR   EnsemblBacteria; GAT74733; GAT74733; MHM582_3241.
DR   Proteomes; UP000077073; 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   Complete proteome {ECO:0000313|Proteomes:UP000077073};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077073}.
FT   DOMAIN      159    287       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      371    440       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     167    174       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   464 AA;  51987 MW;  44ADBE1F014A80EB CRC64;
     MSSPAQPDVP IWTTVQELLE ADDRVTPQLQ GFLSLAVPAG VMAATLYLEV PNDLTAAQIN
     KRLRLPIMEA LSHVGDEVTS YRVVVNHELA EQPNSPIAVP DFGRQDQSRT ESPMEQQPTP
     IRHESRLNPK YTFDNFVIGQ SNRFAHAAAV AVAEAPAKAY NPLFIYGDSG LGKTHLLHAI
     GDYAQSLYAG VKVRYVSSEE FTNDFINSIA NNRGAAFQAR YREVDILLID DIQFLQGRAE
     TQEAFFHTFN TLHDHNKQVV ITSDVAPKLL TGFEDRMRSR FEWGLITDVQ APDLETRIAI
     LRKKAQSESL HIPDEVLEYI ATVVSSNIRE LEGALIRVSA FASLNRSALD ISLAQTVLRD
     IIDTAEDNII SPTDIITATA QYFKLTVDDL YGSSRSQQIA TARQIAMYLC RERTSLSLPK
     IGQLFGNRDH TTVMYAYKKI SELMKERRSI YNQVTEITTQ LGRR
//
DBGET integrated database retrieval system