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Database: UniProt
Entry: A0A136N629_9BACT
LinkDB: A0A136N629_9BACT
Original site: A0A136N629_9BACT 
ID   A0A136N629_9BACT        Unreviewed;       480 AA.
AC   A0A136N629;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   25-OCT-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=UZ11_BCD004001903 {ECO:0000313|EMBL:KXK41621.1};
OS   Bacteroidetes bacterium OLB11.
OC   Bacteria; Bacteroidetes.
OX   NCBI_TaxID=1617422 {ECO:0000313|EMBL:KXK41621.1, ECO:0000313|Proteomes:UP000070496};
RN   [1] {ECO:0000313|EMBL:KXK41621.1, ECO:0000313|Proteomes:UP000070496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB11 {ECO:0000313|EMBL:KXK41621.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-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:KXK41621.1}.
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DR   EMBL; LNFQ01000062; KXK41621.1; -; Genomic_DNA.
DR   PATRIC; fig|1617422.3.peg.2069; -.
DR   Proteomes; UP000070496; 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:UP000070496};
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:UP000070496}.
FT   DOMAIN      174    304       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      385    454       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     182    189       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   480 AA;  54950 MW;  3B8FCC4E7BE735D3 CRC64;
     MIKTHETVWE NCLKIIKDNI HWQSYNTWFE PIKPVKLEGN TLVIEVPSQF FYEWLEENYV
     ELIAKTIKRE LGKDAKLEYL ILMEASTKNN PSSVRVSASN QQPAQLSNNY VDIHLGGRNE
     SGIKNPFVIP GLKRSQIDPQ LNPNNTFDSF IEGECNKLAR SAGLAVSQKP GGTAFNPLVI
     YSAAGLGKTH LVHAIGNETK RLHPNKTVLY VSAEKFIHQF IEHSKNNEIN DFINFYQLID
     VLIIDDVHYF IPAAKSQDAF FSIFNHLHQN GKQLILTSDK PPKDLEGMQE RLLSRFRWGL
     CADLQMPDFE TRKEILEHKM KRDGLDLPVE VVKYLAYNVQ NNIREMEGAL ISLLANASLV
     KKEIDLELAK KVLKNIVKTS TKELTIENIQ KMVCDFYAIP YDKLQAKTRK REIVQARQIS
     MFLSKQYTKN SLKTIGEHFG GRDHTTVIHS CQTVKNLMDT DSLIRDQVKD LQQKVQLATI
//
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