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Database: UniProt
Entry: D5V9C3_MORCB
LinkDB: D5V9C3_MORCB
Original site: D5V9C3_MORCB 
ID   D5V9C3_MORCB            Unreviewed;       467 AA.
AC   D5V9C3;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   25-OCT-2017, entry version 53.
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   ECO:0000313|EMBL:ADG60276.1};
GN   OrderedLocusNames=MCR_0002 {ECO:0000313|EMBL:ADG60276.1};
OS   Moraxella catarrhalis (strain BBH18).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Moraxella.
OX   NCBI_TaxID=1236608 {ECO:0000313|Proteomes:UP000000930};
RN   [1] {ECO:0000313|EMBL:ADG60276.1, ECO:0000313|Proteomes:UP000000930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BBH18 {ECO:0000313|EMBL:ADG60276.1,
RC   ECO:0000313|Proteomes:UP000000930};
RX   PubMed=20453089; DOI=10.1128/JB.00121-10;
RA   de Vries S.P., van Hijum S.A., Schueler W., Riesbeck K., Hays J.P.,
RA   Hermans P.W., Bootsma H.J.;
RT   "Genome analysis of Moraxella catarrhalis strain RH4, a human
RT   respiratory tract pathogen.";
RL   J. Bacteriol. 192:3574-3583(2010).
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}.
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DR   EMBL; CP002005; ADG60276.1; -; Genomic_DNA.
DR   RefSeq; WP_003667382.1; NC_014147.1.
DR   ProteinModelPortal; D5V9C3; -.
DR   EnsemblBacteria; ADG60276; ADG60276; MCR_0002.
DR   GeneID; 9134690; -.
DR   KEGG; mct:MCR_0002; -.
DR   PATRIC; fig|1236608.7.peg.3; -.
DR   HOGENOM; HOG000235659; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000000930; Chromosome.
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:UP000000930};
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:UP000000930}.
FT   DOMAIN      160    296       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      374    443       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     168    175       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   467 AA;  53239 MW;  F180DD49D18B9BC1 CRC64;
     MSLFEDLPVQ DSISPNHLGE RVWQLCLPDL QFAMADKDYR QWIAPLKAEV NDTELLLLAP
     NMMWVRHVKD NYLSQITDLA YQHGKGVIKS VRIEMVASTI PNDPATKKAK TNKKTSKKTG
     VVEGLPIDPG FTFDVFIKGK SNASAYNACN ELSRKESKHN YGPIFIYGSS GLGKTHLMHA
     MAHRYQKYGK QFFYFTKDHF YKITLEAFRT NDIVQMEKEI CQADLLIIDD VHMVSGSKAP
     KVTEILMKLF DAFSAGNTQK QVVLASDRPP SQMTSFGERY ISRLSSCLQL SIEPPDMEMR
     IQILEKKAQM LNLLLPRECA LYMAQNLPPD VRGLEGALKR VQLSATILRN EPVSLPLVKD
     AIKDQVQARA RALNAENIRD LVAEYYEISP KDLMSKKRAR YIARPRQMAM ALIRELTRDS
     FPEIGQVFGG RDHTTVMHAC EKIEELRTQD AKIQKDYHSL KMMLEYV
//
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