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Database: UniProt
Entry: A0A0P6SJB5_9STRE
LinkDB: A0A0P6SJB5_9STRE
Original site: A0A0P6SJB5_9STRE 
ID   A0A0P6SJB5_9STRE        Unreviewed;       451 AA.
AC   A0A0P6SJB5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 18.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=AKK44_05200 {ECO:0000313|EMBL:KPJ22337.1};
OS   Streptococcus phocae.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=119224 {ECO:0000313|EMBL:KPJ22337.1, ECO:0000313|Proteomes:UP000049578};
RN   [1] {ECO:0000313|EMBL:KPJ22337.1, ECO:0000313|Proteomes:UP000049578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51973 {ECO:0000313|EMBL:KPJ22337.1,
RC   ECO:0000313|Proteomes:UP000049578};
RA   Avendano-Herrera R.;
RT   "Genome sequence of Streptococcus phocae subsp. phocae ATCC 51973T
RT   isolated from liver specimen obtained from seal.";
RL   Submitted (AUG-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:SAAS00735475}.
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:KPJ22337.1}.
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DR   EMBL; LHQM01000019; KPJ22337.1; -; Genomic_DNA.
DR   RefSeq; WP_054278804.1; NZ_LHQM01000019.1.
DR   EnsemblBacteria; KPJ22337; KPJ22337; AKK44_05200.
DR   PATRIC; fig|119224.3.peg.579; -.
DR   Proteomes; UP000049578; 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; 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   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:UP000049578};
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:UP000049578}.
FT   DOMAIN      144    277       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      360    429       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     152    159       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   451 AA;  51710 MW;  0EC17B6E7F66D077 CRC64;
     MTENEQIFWN RVLELAQSQL KQATYEFFVH DARLLKVENH VATIYLDQMK ELFWEKNLKD
     VILTAGFEIF NAQITVEYVF EEDLVIEQRQ SQPNYQYQPQ VAPQLPAVKS DLNSKYSFDN
     FIQGDENRWA VAASIAVANT PGTTYNPLFI WGGPGLGKTH LLNAIGNSVL LENPNARIKY
     ITAENFINEF VIHIRLDTMD ELKEKFRNLD LLLIDDIQSL AKKTLSGTQE EFFNTFNALH
     NNNKQIVLTS DRTPDHLNDL EDRLVTRFKW GLTVNITPPD FETRVAILTN KIQDYTFTFP
     QDTIEYLAGQ FDSNVRDLEG ALKDISLVAN FKQIDTITVD VAAEAIRARK QDGPKMTVIP
     IEDIQVQVGK FYDVTVKEIK ATKRTQDIVL ARQVAMFLAR EMTDNSLPKI GKEFGGRDHS
     TVLHAYNKIK NMIAQDDSLR IEIETIKNKI K
//
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