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Database: UniProt
Entry: K8ZKS3_9ENTE
LinkDB: K8ZKS3_9ENTE
Original site: K8ZKS3_9ENTE 
ID   K8ZKS3_9ENTE            Unreviewed;       464 AA.
AC   K8ZKS3;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   05-JUL-2017, entry version 34.
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=C683_0956 {ECO:0000313|EMBL:EKU27178.1};
OS   Catellicoccus marimammalium M35/04/3.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Catellicoccus.
OX   NCBI_TaxID=1234409 {ECO:0000313|EMBL:EKU27178.1, ECO:0000313|Proteomes:UP000016057};
RN   [1] {ECO:0000313|EMBL:EKU27178.1, ECO:0000313|Proteomes:UP000016057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M35/04/3 {ECO:0000313|EMBL:EKU27178.1,
RC   ECO:0000313|Proteomes:UP000016057};
RX   PubMed=23405330;
RA   Weigand M.R., Ryu H., Bozcek L., Konstantinidis K.T.,
RA   Santo Domingo J.W.;
RT   "Draft Genome Sequence of Catellicoccus marimammalium, a Novel Species
RT   Commonly Found in Gull Feces.";
RL   Genome Announc. 1:E00019-12(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:SAAS00731907}.
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:EKU27178.1}.
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DR   EMBL; AMYT01000019; EKU27178.1; -; Genomic_DNA.
DR   RefSeq; WP_009491363.1; NZ_AMYT01000019.1.
DR   EnsemblBacteria; EKU27178; EKU27178; C683_0956.
DR   PATRIC; fig|1234409.3.peg.907; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000016057; 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; 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   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:UP000016057};
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:UP000016057}.
FT   DOMAIN      132    265       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      363    432       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     140    147       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   464 AA;  53474 MW;  6D1D3CF51FB413FD CRC64;
     MLPTTQDSIW SDFQQKCLEN ISSASLRHWI EPAHIVEFDE EHITLSLPAD YIIDHWKMKL
     EPVLKEVCYN YTGKEIEVSY LLSSTPQVQQ EVAKVKNSSI NGDYTFQNFV CGKNNRMAFT
     AANAVVERPG DLYNPLFLYG PSGLGKTHLM HAIANELLAK NPNANIKLIP SETFINEFTK
     IASQSNNTVA LSNFREKYRN VDALFIDDIQ FFIDKTKTQD EFFYTFEELY NSKKQIVLTS
     DRSIKELDKF DERLSSRCGM GTRANIESPD FETRIKILHK KSLDLGLNLE DSALHYIASK
     YDRNVRDLES ALKSIMLYLH SELQMDNYNE IINLAMVKAA LQHEVGSPQI IPLMESIPDN
     EINYQQIQEL VADYYHISLE ELLGKGRAKK YSQPRQIAMY LIRKELQLPF DKIAVIFNRK
     DHTTIMYSIE KIEKNMKQDE ALAEDISTLE QQLSTSVIHN IVDN
//
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