GenomeNet

Database: UniProt
Entry: A0A0R1ZKU0_9LACO
LinkDB: A0A0R1ZKU0_9LACO
Original site: A0A0R1ZKU0_9LACO 
ID   A0A0R1ZKU0_9LACO        Unreviewed;       444 AA.
AC   A0A0R1ZKU0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   05-JUL-2017, entry version 15.
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=FC18_GL001198 {ECO:0000313|EMBL:KRM55581.1};
OS   Lactobacillus sharpeae JCM 1186 = DSM 20505.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1291052 {ECO:0000313|EMBL:KRM55581.1, ECO:0000313|Proteomes:UP000051679};
RN   [1] {ECO:0000313|EMBL:KRM55581.1, ECO:0000313|Proteomes:UP000051679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20505 {ECO:0000313|EMBL:KRM55581.1,
RC   ECO:0000313|Proteomes:UP000051679};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O.,
RA   Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E.,
RA   Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R.,
RA   Caufield P.W., Cui Y., Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through
RT   comparative genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:SAAS00731907}.
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}.
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:KRM55581.1}.
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; AYYO01000017; KRM55581.1; -; Genomic_DNA.
DR   RefSeq; WP_056975623.1; NZ_AYYO01000017.1.
DR   EnsemblBacteria; KRM55581; KRM55581; FC18_GL001198.
DR   PATRIC; fig|1291052.5.peg.1216; -.
DR   Proteomes; UP000051679; Unassembled WGS sequence.
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; 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   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:UP000051679};
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:UP000051679}.
FT   DOMAIN      139    270       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      350    419       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     147    154       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   444 AA;  49816 MW;  CBCB3E1A0DD48351 CRC64;
     MDELWAYITD HFRENMSSVA YTTWIESATP VRLNADTLEI QVPDQLHQTY WQKNLAVKVV
     EAAYSFNGTE LSPVITIKGD EPETTPEPEA EVQTAAPTPT FKTVSHLNSR YTFEDFVIGK
     GNQMAHAAAL AVSDEPGTLY NPLFLYGGVG LGKTHLMQAI GHHMLQNNPN ANVKYVSGED
     FTNDFINSIQ SKRQEQFRQE YRNVDLLLVD DIQFFGDKEG TQEEFFHTFN ALFNSKKQIV
     LTSDRLPNEI PKLQDRLVSR FKWGLSVDIT PPDLETRIAI LRNKATDEGL DAPEDTLHYI
     AGQIDSNVRE LEGALLRVKI FAETTKSPIT TSLAADALKT QISGKNTQLT IAEIQEMVAK
     YYQVSVTDIK GRKRVKQIVM PRQIAMYLAR ELTDSSLPQI GREFGGKDHT TVIHAVDKIE
     KAASADADLK ASIIELKNKL KNRG
//
DBGET integrated database retrieval system