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Database: UniProt
Entry: A0A1G7S0H4_9GAMM
LinkDB: A0A1G7S0H4_9GAMM
Original site: A0A1G7S0H4_9GAMM 
ID   A0A1G7S0H4_9GAMM        Unreviewed;       489 AA.
AC   A0A1G7S0H4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 11.
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=SAMN05216571_10598 {ECO:0000313|EMBL:SDG15580.1};
OS   Halomonas taeanensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=284577 {ECO:0000313|EMBL:SDG15580.1, ECO:0000313|Proteomes:UP000198641};
RN   [1] {ECO:0000313|EMBL:SDG15580.1, ECO:0000313|Proteomes:UP000198641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH539 {ECO:0000313|EMBL:SDG15580.1,
RC   ECO:0000313|Proteomes:UP000198641};
RA   de Groot N.N.;
RL   Submitted (OCT-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: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; FNCI01000005; SDG15580.1; -; Genomic_DNA.
DR   BioCyc; GCF_900100755:BLR71_RS09065-MONOMER; -.
DR   Proteomes; UP000198641; 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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000198641};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198641}.
FT   DOMAIN      186    377       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      397    466       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     194    201       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      348    368       {ECO:0000256|SAM:Coils}.
FT   COILED      466    486       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   489 AA;  54906 MW;  92C223F678D0D88E CRC64;
     MSVALWQQCL DYLQDELSSQ QFNTWIRPLQ AEEGESNELC LLAPNRFVRD WVSDKYAKRI
     SELMRELSPA KPPKVSLTVG SRRAAPAPQP RELGNPVSAG SRPEQAAPAV HTPPRGDYAD
     EREIDQMRDE GARRPAGSTR QVQVEGSLKH QSGLNPNFTF ETFVEGKSNQ LARAASRQVS
     ENPGGAYNPL FLYGGVGLGK THLMHAVGNQ LAGRSENAKV VYLHSERFVA DMVKALQLNA
     INDFKRFYRS VDALLIDDIQ FFAGKERSQE EFFHTFNALL EGGQQMILTS DRYPKEISGV
     EERLKSRFGW GLTVAIEPPE LETRVAILMK KADQAKVDLP HDAAFFIAQK IRSNVRELEG
     ALKKVIADSH FMGKTITQDF IRESLKDLLA LQDKQVGVDN IQRTVAEYYK IKLADLLSKR
     RSRSVARPRQ VAMALAKELT NHSLPEIGDA FGGRDHTTVL HACRKVQALQ EENADIREDY
     KNLLRLLTS
//
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