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Database: UniProt
Entry: Q040E9_LEUMM
LinkDB: Q040E9_LEUMM
Original site: Q040E9_LEUMM 
ID   Q040E9_LEUMM            Unreviewed;       448 AA.
AC   Q040E9;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   05-JUL-2017, entry version 92.
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   OrderedLocusNames=LEUM_0001 {ECO:0000313|EMBL:ABJ61173.1};
OS   Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 /
OS   NCDO 523).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=203120 {ECO:0000313|EMBL:ABJ61173.1, ECO:0000313|Proteomes:UP000000362};
RN   [1] {ECO:0000313|EMBL:ABJ61173.1, ECO:0000313|Proteomes:UP000000362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8293 / NCDO 523 {ECO:0000313|Proteomes:UP000000362};
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V.,
RA   Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R.,
RA   Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F.,
RA   Broadbent J., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.,
RA   Klaenhammer T., Richardson P., Kozyavkin S., Weimer B., Mills D.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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:SAAS00756131}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
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DR   EMBL; CP000414; ABJ61173.1; -; Genomic_DNA.
DR   RefSeq; WP_002816101.1; NC_008531.1.
DR   ProteinModelPortal; Q040E9; -.
DR   STRING; 203120.LEUM_0001; -.
DR   EnsemblBacteria; ABJ61173; ABJ61173; LEUM_0001.
DR   GeneID; 29576793; -.
DR   KEGG; lme:LEUM_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000000362; Chromosome.
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; IPR024633; DnaA_N_dom.
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   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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000362};
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:UP000000362}.
FT   DOMAIN      141    277       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      354    423       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     149    156       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   448 AA;  50062 MW;  0B4A36AB219EE40A CRC64;
     MTKPITKEEL WSKVQAEFFT KLGRVTFSTY IEPLKPLTLG DTSLTLAVPS DMAQDIIDQW
     DSEYSMDFVQ FAMSIADGFI KPDLQVAEAK PTTIPTFSDN LSFTRESDLN PDFTFEKFVI
     GSGNENAYAV ARAVADEPGQ VYNPYLIYGG VGLGKTHLMQ AIGNAYAVST PSAHIKYATA
     EDFLNDFTES LRAGDGATAA FKQEYRSVDL LLVDDIQFWS GKEKVQEEFF NTFNVLTKNG
     KQIVMTSDKL PTEIVDLQTR LTSRFEAGIM MDIQKPDLPT RVAILQNLSE SDGLDIPNDV
     LELIAEKIDS NVRSLEGAFH KFEASLRYMN KPATKETAQQ ILGDLNINQG FKITVERIQQ
     VVADYYMQTI DDLKSSSRKK DLVTARHVAM YLTRTLTNES LPDIGRSFGG RDHSSVLHAT
     TKITEKSESD SRTKEMLDAL TDEIKHGK
//
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