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Database: UniProt
Entry: A0A1Y0H2Z6_9BACT
LinkDB: A0A1Y0H2Z6_9BACT
Original site: A0A1Y0H2Z6_9BACT 
ID   A0A1Y0H2Z6_9BACT        Unreviewed;       458 AA.
AC   A0A1Y0H2Z6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   16-JAN-2019, entry version 12.
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=CCB80_15280 {ECO:0000313|EMBL:ARU42439.1};
OS   Armatimonadetes bacterium Uphvl-Ar1.
OC   Bacteria; Armatimonadetes.
OX   NCBI_TaxID=2004467 {ECO:0000313|EMBL:ARU42439.1};
RN   [1] {ECO:0000313|EMBL:ARU42439.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Uphvl-Ar1 {ECO:0000313|EMBL:ARU42439.1};
RA   Woodhouse J.N., Makower A.K., Ionescu D., Grossart H.-P., Neilan B.A.,
RA   Dittmann E.;
RT   "Draft genome sequences of three Uncultured Armatimonadetes, binned
RT   from a Microcystis sp. enrichment culture and from Microcystis bloom
RT   metagenomes.";
RL   Submitted (MAY-2017) 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}.
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DR   EMBL; CP021423; ARU42439.1; -; Genomic_DNA.
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   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}.
FT   DOMAIN      152    280       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      364    433       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     160    167       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   458 AA;  51838 MW;  DB36DC103A051BA3 CRC64;
     MSDQHTLMDH EDLVVLKTAW ESSLRDLKGQ VPETVLTRFL KKLEPIEYRD ERVVFAAPGR
     FVHDWVKDRY VDRLQTSLSE KLQKSIKFEL KIASSERQAP SNHAVAAVTP RASEPSRFKP
     IERLTFDNFV QGQSNRLAFA GAKAVADNPG TRFNPLFIYG PSGLGKTHLL HAIANEILGR
     DPYHSIMYVT AAQFMEDFVT ALKNNQIERF RRQQRGVNVW LLDDVQYVAG KDKTLEEIFH
     TFNYLQSLGK QIVLCSDRPP RDLLLMDERL RSRFESGLVV DVQHPDTETK CAILLKRADV
     EGIAIDQETA MAIAEGVNGT VRHLEGALHK LAAQSSLTGQ PINAELAAEI VERYYANLVV
     AKPSFEQIVG SVSKHYRVES DEILGISRKA HIATARHVAI YITREILGDS WKQIGAMFGN
     KDHTSMMHGY KKVRTMMNQS REMNASIRAL INDLYPNQ
//
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