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Database: UniProt
Entry: A0A0R1RFY9_9LACO
LinkDB: A0A0R1RFY9_9LACO
Original site: A0A0R1RFY9_9LACO 
ID   A0A0R1RFY9_9LACO        Unreviewed;       438 AA.
AC   A0A0R1RFY9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 18.
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:CUS25309.1};
GN   ORFNames=FC70_GL001306 {ECO:0000313|EMBL:KRL55702.1}, LACOL_0001
GN   {ECO:0000313|EMBL:CUS25309.1};
OS   Lactobacillus oligofermentans DSM 15707 = LMG 22743.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1423778 {ECO:0000313|EMBL:KRL55702.1, ECO:0000313|Proteomes:UP000051697};
RN   [1] {ECO:0000313|EMBL:KRL55702.1, ECO:0000313|Proteomes:UP000051697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15707 {ECO:0000313|EMBL:KRL55702.1,
RC   ECO:0000313|Proteomes:UP000051697};
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).
RN   [2] {ECO:0000313|EMBL:CUS25309.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LACOL {ECO:0000313|EMBL:CUS25309.1};
RA   Millard Andrew;
RL   Submitted (OCT-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}.
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DR   EMBL; LN898144; CUS25309.1; -; Genomic_DNA.
DR   EMBL; AZFE01000031; KRL55702.1; -; Genomic_DNA.
DR   RefSeq; WP_057890228.1; NZ_AZFE01000031.1.
DR   EnsemblBacteria; KRL55702; KRL55702; FC70_GL001306.
DR   PATRIC; fig|1423778.4.peg.1340; -.
DR   Proteomes; UP000051697; 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:UP000051697};
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:UP000051697}.
FT   DOMAIN      135    266       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      346    415       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     143    150       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   438 AA;  49752 MW;  57D654889750FDEC CRC64;
     MTDLESFWNK IKESFKNDVT SVTYNNLIDP AKIISFDDDL LTIELPSTFH KDYWVKSLTP
     KVQQYTFKEI GKNVTPYYIV ESDQPTNHVP SKDTRSFKVD TALNPRYTFD TYVIGKGNQM
     AHAAALVVSE EPGKMYNPLF FYGGVGLGKT HLMHAIGNKM MEANSNTRVK YVTSEAFTND
     FINAIQTGQQ EQFRQEYRQL DLLLVDDIQF FADKEGTQEE FFHTFNALYE ENKQIVLTSD
     RLPNEIPKLQ DRLVSRFKWG LSVDITTPDL ETRIAILRSK AQADHIDIPS DTLTYIASQV
     DSNVRELEGA LSRVQAYSHL MKKSITTELA ANSLKALKLE GVQTLTVEVI QEKVAAYYSL
     SVADLRGKKR VKQIVVPRQI AMFLARDLTD YSLPKIGDAF GGKDHSTVLH SIDKIEAEIK
     TNANLQEDVQ NLKIELKP
//
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