GenomeNet

Database: UniProt
Entry: Z9JP53_9MICO
LinkDB: Z9JP53_9MICO
Original site: Z9JP53_9MICO 
ID   Z9JP53_9MICO            Unreviewed;       561 AA.
AC   Z9JP53;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   25-OCT-2017, entry version 30.
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=BF93_05005 {ECO:0000313|EMBL:EWS80200.1};
OS   Brachybacterium phenoliresistens.
OC   Bacteria; Actinobacteria; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=396014 {ECO:0000313|EMBL:EWS80200.1, ECO:0000313|Proteomes:UP000023067};
RN   [1] {ECO:0000313|EMBL:EWS80200.1, ECO:0000313|Proteomes:UP000023067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W13A50 {ECO:0000313|EMBL:EWS80200.1,
RC   ECO:0000313|Proteomes:UP000023067};
RA   Wang X.;
RT   "Genome sequence of Brachybacterium phenoliresistens strain W13A50.";
RL   Submitted (FEB-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:EWS80200.1}.
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; JDYK01000018; EWS80200.1; -; Genomic_DNA.
DR   RefSeq; WP_038373834.1; NZ_KK070001.1.
DR   EnsemblBacteria; EWS80200; EWS80200; BF93_05005.
DR   PATRIC; fig|396014.3.peg.3031; -.
DR   Proteomes; UP000023067; 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:UP000023067};
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:UP000023067}.
FT   DOMAIN      246    377       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      462    531       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     254    261       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   561 AA;  62673 MW;  22AB9D6A0C910AC9 CRC64;
     MDDSTLDLDA TWDETLRVLR REDEVNERAM AFLTLSRLMA VVADTALLAV PSSWAKDVFE
     QRYAAALSSA LTQAVGRETR FAVTIDATLL MSGSEDEDRP ATSSPAPAPR RESAVDDAVD
     NPPLRRPEPR EHREPRESRE PREASSPRGR EERVREDDDS PFAERPARPE PVRDDEPAAL
     FERRHLQQRP ASAASPHPAP QDGGDSTLGS DSRLNAKYTF ETFVIGASNR FAQAAASAVA
     EAPAKAYNPL FIYGGSGLGK THLLHAVGHY AQSMYSGIEV RYVNSEEFTN DFINSVQSGQ
     FGKAQEFHRR YRDIDILLID DIQFLQRAPE TMEAFFHTFN TLHNADKQIV ITSDLPPKQL
     GGFEDRMRSR FEMGLMTDVQ PPDLETRIAI LRKKVEMENT QEVPRDVLEY IASRISTNIR
     ELEGALIRVQ ALHSLSRQPM DVSLAESVLK DLLTHDSGAE ITAATIIAQT AAYFGLTVDQ
     VTGGARTRVL VTARQIAMYL CRELTDMPLI RIGKEFGGRD HTTVMHANKK IAELMKERRA
     IFNQVTELTA RIKNSSADQV R
//
DBGET integrated database retrieval system