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Database: UniProt
Entry: E2SHL6_9FIRM
LinkDB: E2SHL6_9FIRM
Original site: E2SHL6_9FIRM 
ID   E2SHL6_9FIRM            Unreviewed;       452 AA.
AC   E2SHL6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   25-OCT-2017, entry version 45.
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   ECO:0000313|EMBL:EFP62968.1};
GN   ORFNames=HMPREF0983_00466 {ECO:0000313|EMBL:EFP62968.1};
OS   Erysipelotrichaceae bacterium 3_1_53.
OC   Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae.
OX   NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP62968.1, ECO:0000313|Proteomes:UP000006223};
RN   [1] {ECO:0000313|EMBL:EFP62968.1, ECO:0000313|Proteomes:UP000006223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_53 {ECO:0000313|EMBL:EFP62968.1,
RC   ECO:0000313|Proteomes:UP000006223};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q.,
RA   Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Howarth C., Jen D., Larson L., Mehta T.,
RA   Neiman D., Park D., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   Allen-Vercoe E., Strauss J., Sibley C., Daigneault M., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53.";
RL   Submitted (JUL-2010) 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:EFP62968.1}.
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DR   EMBL; ACTJ01000011; EFP62968.1; -; Genomic_DNA.
DR   RefSeq; WP_009271514.1; NZ_GL520133.1.
DR   STRING; 658659.HMPREF0983_00466; -.
DR   EnsemblBacteria; EFP62968; EFP62968; HMPREF0983_00466.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   Proteomes; UP000006223; 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:UP000006223};
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:UP000006223}.
FT   DOMAIN      144    277       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      359    428       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     152    159       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   452 AA;  52190 MW;  3ED37403D32031CA CRC64;
     MSNFAKVQLE QIWQKTLQLI NESAHFDDAV FNAWYKEDSH LFDIEDDFAT IVVPYKINKQ
     IMMDSIDLIQ QKLSDVLDMK VSCQILLKSE VDMLQPSSVV KRRNEILFED KVKKEYTFDS
     FVVGKNNREA HAAALSVCYY PGKFNNPLFI FGNSGLGKTH LLHAIGNYVK ANRPEEKVLY
     IYSEDFVTLL IEAMKNKTVE DVKEMICSVD YLLIDDIQRL KQSTSQEIFF NMYNKLISDN
     KQIVITSDIH PTELKGIENR LISRFSSGLS VSVGSPEFET AKAILQKKME GRSDEIMIDD
     EVLDFLATRF ASDVRKLEGT LNELFFKAIL YNPERIDITF AKEIFKENPI VVKQEDELTP
     KRIKNAVCEY YGLTRTQIES KSRTKNIANA RHIAIYLCRT HLEMPFAKIG FEFGNRDHST
     IMSSYEKMMK LLKEKETFQQ AVMQIESSLG IK
//
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