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Database: UniProt
Entry: L8JH16_9BACT
LinkDB: L8JH16_9BACT
Original site: L8JH16_9BACT 
ID   L8JH16_9BACT            Unreviewed;       472 AA.
AC   L8JH16;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   05-JUL-2017, entry version 31.
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=C900_00732 {ECO:0000313|EMBL:ELR68156.1};
OS   Fulvivirga imtechensis AK7.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Fulvivirga.
OX   NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR68156.1, ECO:0000313|Proteomes:UP000011135};
RN   [1] {ECO:0000313|EMBL:ELR68156.1, ECO:0000313|Proteomes:UP000011135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK7 {ECO:0000313|EMBL:ELR68156.1,
RC   ECO:0000313|Proteomes:UP000011135};
RA   Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Fulvivirga imtechensis AK7.";
RL   Submitted (DEC-2012) 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:SAAS00756131}.
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:ELR68156.1}.
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DR   EMBL; AMZN01000139; ELR68156.1; -; Genomic_DNA.
DR   RefSeq; WP_009583654.1; NZ_AMZN01000139.1.
DR   EnsemblBacteria; ELR68156; ELR68156; C900_00732.
DR   PATRIC; fig|1237149.3.peg.5800; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000011135; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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:UP000011135};
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:UP000011135}.
FT   DOMAIN      166    296       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      377    446       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     174    181       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   472 AA;  53759 MW;  44D1989CF0229A08 CRC64;
     MHIDCETVWG DCLRVIKENV ADQSFNTWFK PIVPLKCSND VLTIQVPSQF FYEWLEEHYV
     HVLKKAITAV MGTQARLEYS VIVDKGNSKS SPLSVSLPNR TQAKNFGSNG AKEEYISPFQ
     LKSVDSLYQE SQLNPNNTFD SYIEGDCNRL ARSAGYAVAQ KPGVTSFNPL MLYGGVGLGK
     THLVQAIGNE IKNNLSDRFV LYVSSEKFTN QFIDALRNNK TQEFQNFYMQ VDILIIDDVQ
     FLAGKERTQE IFFHIFNHLH QAGKQIVMTS DCPPRDLKGL QERLLSRFKW GLTADLQQPD
     YETRVAIIQR KMQTDGIYIP DNVIEYLAYS VDTNIRELEG VLISLIAHAS LNRVDIDLEL
     AKQTLKNIVH DIETEVGIDY IQKTVAEYFK VEVASLKDKI RKKEIVIARQ VAMYFAKEYT
     NHSLKAIGYH FGGRDHSTVI HAVQSVNDMM DTNASFKSSV EELKKKLKMK AI
//
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