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Database: UniProt
Entry: K4KKX2_SIMAS
LinkDB: K4KKX2_SIMAS
Original site: K4KKX2_SIMAS 
ID   K4KKX2_SIMAS            Unreviewed;       468 AA.
AC   K4KKX2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-SEP-2017, entry version 41.
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:AFU99646.1};
GN   OrderedLocusNames=M5M_12450 {ECO:0000313|EMBL:AFU99646.1};
OS   Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 /
OS   SA1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Simiduia.
OX   NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFU99646.1, ECO:0000313|Proteomes:UP000000466};
RN   [1] {ECO:0000313|EMBL:AFU99646.1, ECO:0000313|Proteomes:UP000000466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC   {ECO:0000313|Proteomes:UP000000466};
RX   PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA   Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT   "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT   bacterium able to degrade a variety of polysaccharides.";
RL   Genome Announc. 1:E00039-E00039(2013).
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:SAAS00756131}.
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; CP003746; AFU99646.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFU99646; AFU99646; M5M_12450.
DR   KEGG; saga:M5M_12450; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000000466; 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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000466};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000466}.
FT   DOMAIN      165    295       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      376    445       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     173    180       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   468 AA;  52521 MW;  6676AE0237D9472E CRC64;
     MPETIWNQCV TSLQNELSPE QFNTWIRPLQ LDVSAGHAQL TLLAPNQFIK SWVSDKFLPR
     IAELVSSQAG DSIEVVLGVA NRQQPAVRSR ATSPVSQDAV QVREVVAPEP ARATAPQERA
     ANVDGGLKHQ HRLNTQFTFP RFVEGKSNQL GLAAARQVAE NPGGAYNPLF IYGGVGLGKT
     HLMHAVGNAM LERNPNAKIL YLHSERFVAD MVKALQLNAI NDFKRYYRSL DALLIDDIQF
     FAGKERSQEE FFHTFNALLE GGQQIILTCD RYPREIEGLE ERLKSRFGWG LTVAVEPPEL
     ETRVAILMKK ATQQNLTLPH DAAFFIAQRI RSNVRELEGA LKRVVANASF TGRPIDVELV
     RESLKDLLAL QDKQVSIDNI QRVVAEYYKI KVSDLHSKRR SRSVARPRQV AMSLAKELTN
     HSLPEIGEAF GGRDHTTVLH ACRKIKELQE ESADIREDTK NLQRLLTS
//
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