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Database: UniProt
Entry: A0A0R2UCN7_9CYAN
LinkDB: A0A0R2UCN7_9CYAN
Original site: A0A0R2UCN7_9CYAN 
ID   A0A0R2UCN7_9CYAN        Unreviewed;       463 AA.
AC   A0A0R2UCN7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 13.
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=ABR96_05445 {ECO:0000313|EMBL:KRO94733.1};
OS   cyanobacterium BACL30 MAG-120619-bin27.
OC   Bacteria; Cyanobacteria.
OX   NCBI_TaxID=1655601 {ECO:0000313|EMBL:KRO94733.1, ECO:0000313|Proteomes:UP000051566};
RN   [1] {ECO:0000313|EMBL:KRO94733.1, ECO:0000313|Proteomes:UP000051566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL30 MAG-120619-bin27 {ECO:0000313|EMBL:KRO94733.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C.,
RA   Pinhassi J., Andersson A.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
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}.
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:KRO94733.1}.
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DR   EMBL; LICO01000005; KRO94733.1; -; Genomic_DNA.
DR   Proteomes; UP000051566; 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:UP000051566};
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:UP000051566}.
FT   DOMAIN      156    289       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      365    434       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     164    171       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   463 AA;  51221 MW;  8F85730CA439A9E0 CRC64;
     MQQGEELWHQ VQQALQANLS KPTFETWIRP ARCLGFEAGQ LQLEAPNSFA CGWLRKNYLG
     TIEAVASEIA GRPVQVRVSA ASGDDVIAAA ASGAETAMAP VALASRDTAP RATGETPRKL
     APGLNPRYVF NRFVVGPNSR MAHAAALAVA EAPGREFNPL FLCGGVGLGK THLMQAIGHY
     RLEINPDARV FYVSTETFTN DLIQAIRKDG MQAFRDRYRA ADLILVDDIQ FIEGKEYTQE
     EFFHTFNALH EAGRQIVIAS DRPPSQIPRL QERLISRFSM GLIADIQVPD LETRMAILHK
     KAEQEQMVLP RDLIQFIAGR FTSNIRELEG ALTRAVAFAS ITGLPMTVES VAPMLDPGGW
     DVEVKPGQVI EKVAEVFGVG VEEMRSASRK RAVSQARQVG MYLMRQSTNL SLPRIGEAFG
     GKDHSTVMYA VEQIDRKLNS DPALSRQVQQ VRDLLQIDSR KRR
//
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