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Database: UniProt
Entry: A0A0R2FLF1_9LACO
LinkDB: A0A0R2FLF1_9LACO
Original site: A0A0R2FLF1_9LACO 
ID   A0A0R2FLF1_9LACO        Unreviewed;       470 AA.
AC   A0A0R2FLF1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-SEP-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   ORFNames=IV38_GL000814 {ECO:0000313|EMBL:KRN28614.1}, IV40_GL001039
GN   {ECO:0000313|EMBL:KRN32976.1};
OS   Lactobacillus selangorensis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=81857 {ECO:0000313|EMBL:KRN28614.1, ECO:0000313|Proteomes:UP000051751};
RN   [1] {ECO:0000313|EMBL:KRN28614.1, ECO:0000313|Proteomes:UP000051645, ECO:0000313|Proteomes:UP000051751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-66 {ECO:0000313|EMBL:KRN28614.1,
RC   ECO:0000313|Proteomes:UP000051751}, and DSM 13344
RC   {ECO:0000313|EMBL:KRN32976.1, ECO:0000313|Proteomes:UP000051645};
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: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}.
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:KRN28614.1}.
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DR   EMBL; JQAT01000002; KRN28614.1; -; Genomic_DNA.
DR   EMBL; JQAZ01000002; KRN32976.1; -; Genomic_DNA.
DR   EnsemblBacteria; KRN28614; KRN28614; IV38_GL000814.
DR   EnsemblBacteria; KRN32976; KRN32976; IV40_GL001039.
DR   PATRIC; fig|81857.3.peg.816; -.
DR   Proteomes; UP000051645; Unassembled WGS sequence.
DR   Proteomes; UP000051751; 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: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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051645,
KW   ECO:0000313|Proteomes:UP000051751};
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:UP000051645}.
FT   DOMAIN      166    297       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      378    447       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     174    181       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      447    470       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   470 AA;  53387 MW;  0A84F07F23D71973 CRC64;
     MIREKEQFLF KMTKKGGINV PNLEELWQYL ESYFQQHLSA VSYSTWIETA KPLKLANHQL
     TIEVPSSLHK DYWEKVLATK VVEGAYAFAN IEITPVFVSK EEEDAQEKAD SDALAAPEVD
     QEANIPTFMR ETRLNSKYTF ETFVTGKGNQ MAHAAALVVS EEPGVLYNPL FLYGGVGLGK
     THLMQAIGHQ LLKTHPGSKV KYVTSEAFAN DFINSIQNKE QEKFRQEYRN VDLLLVDDIQ
     FFADKEGTQE EFFHTFNDLY NNKKQIVLTS DRLPNEIPKL QERLVSRFKW GLSVDITPPD
     LETRIAILRN KANAEHLNIP DDTLSYIAGQ IDSNVRELEG ALVRVQAYAR TKEEPITTSL
     AADALKSLNA EEKPKDLTIT DIQSAVAKYY QVSVADLKGK KRVKNIVWPR QIAMYLSREM
     TDNSLPRIGQ EFGGKDHTTV IHAHEKVAAE LKSDEQLKEQ IAELKNKLKP
//
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