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Database: UniProt
Entry: A0A165U0R8_9GAMM
LinkDB: A0A165U0R8_9GAMM
Original site: A0A165U0R8_9GAMM 
ID   A0A165U0R8_9GAMM        Unreviewed;       492 AA.
AC   A0A165U0R8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-SEP-2017, entry version 12.
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=A3737_01905 {ECO:0000313|EMBL:KZY68101.1};
OS   Oleiphilus sp. HI0065.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oleiphilaceae; Oleiphilus.
OX   NCBI_TaxID=1822241 {ECO:0000313|EMBL:KZY68101.1, ECO:0000313|Proteomes:UP000077382};
RN   [1] {ECO:0000313|EMBL:KZY68101.1, ECO:0000313|Proteomes:UP000077382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI0065 {ECO:0000313|EMBL:KZY68101.1,
RC   ECO:0000313|Proteomes:UP000077382};
RA   Sosa O.A.;
RT   "Microbial cycling of marine high molecular weight dissolved organic
RT   matter.";
RL   Submitted (MAR-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: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:KZY68101.1}.
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DR   EMBL; LWFG01001112; KZY68101.1; -; Genomic_DNA.
DR   RefSeq; WP_068458797.1; NZ_LWFG01001112.1.
DR   EnsemblBacteria; KZY68101; KZY68101; A3737_01905.
DR   Proteomes; UP000077382; 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   Complete proteome {ECO:0000313|Proteomes:UP000077382};
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:UP000077382}.
FT   DOMAIN      189    318       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      400    469       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     197    204       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   492 AA;  55603 MW;  7EC483DF34075309 CRC64;
     MLESVWDNCL ARLEQEESAQ KFNMWLKPLQ AAIVDDVFSL FAPNRFVLDF VNDHYRKRIG
     DLVVELSGKS LPVRVSIGHA PKASSTDNAS QGSVIEADRH AIKNSRISQI SDVSQSRTTS
     ERTSSSFKEN NRALHVSKDA SSSDNKETGV VEHKSALNDK FTFDTFVEGK SNQLARAAAV
     QVADKPGASY NPLFLYGDVG LGKTHLMHAV GNEIKARNPK ARIVYLHSER FVADMVKALQ
     RNDIAKFKKY YRSVDVLLID DIQFFAGKER SQEEFFHTFN ALLEGGQQMI LTCDRYPKEI
     ENMEERLTSR FGWGLSMKLE PPELETRVAI LMRKAEQDNV LLSEESAFFI ANRIRSNVRE
     LEGALKLVAA NANFSGQDIT PAFSQECLKD LLLVHDRQVS VNNIQKTVAE YYKIKVADLL
     SRRRTRSIAR PRQVAMTLSK ELTNHSLPEI GDAFGGRDHT TVLHACRKIA ELKESDANIR
     EEYTNFIRKL TM
//
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