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Database: UniProt
Entry: A0A0F2JFG7_9FIRM
LinkDB: A0A0F2JFG7_9FIRM
Original site: A0A0F2JFG7_9FIRM 
ID   A0A0F2JFG7_9FIRM        Unreviewed;       454 AA.
AC   A0A0F2JFG7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   25-OCT-2017, entry version 19.
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=UF75_1992 {ECO:0000313|EMBL:KJR47642.1};
OS   Desulfosporosinus sp. I2.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1617025 {ECO:0000313|EMBL:KJR47642.1, ECO:0000313|Proteomes:UP000033442};
RN   [1] {ECO:0000313|EMBL:KJR47642.1, ECO:0000313|Proteomes:UP000033442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I2 {ECO:0000313|EMBL:KJR47642.1,
RC   ECO:0000313|Proteomes:UP000033442};
RA   Mardanov A.V., Karnachuk O.V., Beletsky A.V., Kadnikov V.V.,
RA   Ravin N.V.;
RL   Submitted (FEB-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:KJR47642.1}.
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DR   EMBL; JYNH01000029; KJR47642.1; -; Genomic_DNA.
DR   RefSeq; WP_045574318.1; NZ_JYNH01000029.1.
DR   EnsemblBacteria; KJR47642; KJR47642; UF75_1992.
DR   PATRIC; fig|1617025.3.peg.2070; -.
DR   Proteomes; UP000033442; 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:UP000033442};
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:UP000033442}.
FT   DOMAIN      149    277       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      361    430       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     157    164       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   454 AA;  51621 MW;  2F236A50869B5678 CRC64;
     MPPQPLSPQL LWQETLEKLK NELSKPSFET WLSSTRLLHI EGDTLIISVP NDFAKDWLES
     RYAPLIRSSV QAVLGHSVSL RFIIPSPDVS YTEDPVVIKQ QDSSITPKSI DPQHNSLNAK
     YIFDTFVIGN SNRFAHAASL AVAESPAKSY NPLFIYGGVG LGKTHLMHAI GHHVLQRSPN
     TKVLYVSSEK FTNELIDSIR DENSIEFRNH YRNVDILLID DIQFLAGKER TQEEFFHTFN
     ALHEANKQII ISSDRPPKEI PTLEDRLRSR FEWGLITDIQ APDLETRIAI LRKKAKMENL
     QVPNEVMVYI ADKIHSNIRE LEGALIRVMA FASLSSFPIT TEVAVEALKD IIPANNTKQI
     TIENIQQSVA GFFHMPPHEF KAKKRTREVA FPRQIAMYLS RQLTDSSLPK IGEEFGGRDH
     TTVMHAHDKI TQAILNDPLL EKKINEIIQR IQSE
//
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