GenomeNet

Database: UniProt
Entry: A0A0T9KU13_9GAMM
LinkDB: A0A0T9KU13_9GAMM
Original site: A0A0T9KU13_9GAMM 
ID   A0A0T9KU13_9GAMM        Unreviewed;       463 AA.
AC   A0A0T9KU13;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   25-OCT-2017, entry version 15.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:CNE30240.1};
GN   ORFNames=ERS137967_01239 {ECO:0000313|EMBL:CNE30240.1};
OS   Yersinia nurmii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=685706 {ECO:0000313|EMBL:CNE30240.1, ECO:0000313|Proteomes:UP000040578};
RN   [1] {ECO:0000313|EMBL:CNE30240.1, ECO:0000313|Proteomes:UP000040578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=type strain: CIP110231 {ECO:0000313|Proteomes:UP000040578};
RA   Murphy D.;
RL   Submitted (MAR-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:SAAS00724167}.
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CPYD01000003; CNE30240.1; -; Genomic_DNA.
DR   RefSeq; WP_049597411.1; NZ_CPYD01000003.1.
DR   EnsemblBacteria; CNE30240; CNE30240; ERS137967_01239.
DR   Proteomes; UP000040578; 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; IPR024633; DnaA_N_dom.
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   Pfam; PF11638; DnaA_N; 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:UP000040578};
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      160    362       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      371    440       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     168    175       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   463 AA;  52285 MW;  18115283F74CB25A CRC64;
     MSLSLWQQCL ARLQDELPAT EFSMWIRPLQ AELSDNTLAL YAPNRFVLDW VRDKYLNNIN
     GLLNDFCGTN VPLLRFEVGS KPMVQTQNQP VTAASVSAPA APVIRSAPMR PSWDSSPAQP
     ELSYRSNVNP KHTFDNFVEG KSNQLARAAA RQVADNPGGA YNPLFLYGGT GLGKTHLLHA
     VGNGIMARKA NAKVVYMHSE RFVQDMVKAL QNNAIEEFKR YYRSVDALLI DDIQFFANKE
     RSQEEFFHTF NALLEGNQQI ILTSDRYPKE INGVEDRLKS RFGWGLTVAI EPPELETRVA
     ILMKKADEND IRLPGEVAFF IAKRLRSNVR ELEGALNRVI ANANFTGRAI TIDFVREALR
     DLLALQEKLV TIDNIQKTVA EYYKIKVADL LSKRRSRSVA RPRQMAMALA KELTNHSLPE
     IGDAFGGRDH TTVLHACRKI EQLREESHDI KEDFSNLIRT LSS
//
DBGET integrated database retrieval system