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Database: UniProt
Entry: A0A180ERQ1_9BACT
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ID   A0A180ERQ1_9BACT        Unreviewed;       472 AA.
AC   A0A180ERQ1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   16-JAN-2019, entry version 18.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=A3850_010540 {ECO:0000313|EMBL:OAV45880.1};
OS   Lewinella sp. 4G2.
OC   Bacteria; Bacteroidetes; Saprospiria; Saprospirales; Lewinellaceae;
OC   Lewinella.
OX   NCBI_TaxID=1803372 {ECO:0000313|EMBL:OAV45880.1, ECO:0000313|Proteomes:UP000076582};
RN   [1] {ECO:0000313|EMBL:OAV45880.1, ECO:0000313|Proteomes:UP000076582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4G2 {ECO:0000313|EMBL:OAV45880.1,
RC   ECO:0000313|Proteomes:UP000076582};
RA   Wong S.-K., Yoshizawa S., Ogura Y., Tetsuya H., Nakajima Y.,
RA   Hamasaki K.;
RT   "Lewinella sp. 4G2 Genome sequencing.";
RL   Submitted (MAY-2016) 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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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:OAV45880.1}.
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DR   EMBL; LVWJ02000014; OAV45880.1; -; Genomic_DNA.
DR   RefSeq; WP_068219750.1; NZ_LVWJ02000014.1.
DR   EnsemblBacteria; OAV45880; OAV45880; A3850_010540.
DR   Proteomes; UP000076582; 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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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:SAAS00756129};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000076582};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076582}.
FT   DOMAIN      164    291       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      375    444       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     172    179       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      444    471       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   472 AA;  53454 MW;  C1AD16B20BC35241 CRC64;
     MDSNTDHKGL WSQCLQTISQ TVSGQAYETW FAPITPVKLV GNELTIQVPH RLFYEWLEEH
     YVEVLKTSLN TALGEPGRLQ YRINPVKNKV RPTLPQKQGK VTEQVPLTHE NMPGNPFVIP
     GVARPRIPSN LNKGFTFKNF VEGDCNSLAR NAAKAVADNP TQTAFNPLVI HGKSGLGKTH
     LLHAIGNYVN EKYPDKAVLF VGADTFTQHL IDSIASNSTN DLLNWYQNVD ILLVDDIQQL
     VNRKKTQDIF FNLFNVLRQN NKAIVMTCDR PIIELDIEER LRSRFQWGLS ADLSEPALET
     RMAILTSKAH TNNVELPTEV AEFICFHIKN NIRQLEGILH TMVMKKGVAG KEKLDIDLAK
     EVLRSFVSDI NREVTPEVIQ KAVADHFNLD VEKIKSTTRR RQVVLARQIS MFLVKQHTDN
     SLKKIGQLFG NRDHSTVIYS LRAVEDLVDT NDEVRRALAE LERKIRIGKG EG
//
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