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Database: UniProt
Entry: H1YGK3_9SPHI
LinkDB: H1YGK3_9SPHI
Original site: H1YGK3_9SPHI 
ID   H1YGK3_9SPHI            Unreviewed;       475 AA.
AC   H1YGK3;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   05-JUL-2017, entry version 37.
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=Mucpa_1225 {ECO:0000313|EMBL:EHQ25389.1};
OS   Mucilaginibacter paludis DSM 18603.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ25389.1, ECO:0000313|Proteomes:UP000002774};
RN   [1] {ECO:0000313|EMBL:EHQ25389.1, ECO:0000313|Proteomes:UP000002774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ25389.1,
RC   ECO:0000313|Proteomes:UP000002774};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N.,
RA   Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
RL   Submitted (SEP-2011) 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}.
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DR   EMBL; CM001403; EHQ25389.1; -; Genomic_DNA.
DR   RefSeq; WP_008505110.1; NZ_CM001403.1.
DR   STRING; 714943.Mucpa_1225; -.
DR   EnsemblBacteria; EHQ25389; EHQ25389; Mucpa_1225.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000002774; Chromosome.
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:UP000002774};
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:UP000002774}.
FT   DOMAIN      171    301       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      382    451       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     179    186       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   475 AA;  53921 MW;  1AB9E482A0C8BD8C CRC64;
     MEKTCTNVWN SCLQIIKDNI PAQSFKTWFE PIKALRIEGS VLTIQVPSLF FFEWLEEHYV
     GLLRKTIKKQ LGEDGRLEYN IVVEQSSSSK PYTTNMPSNG NGAEGKNQSM PIPISINKDI
     KNPFVIPGLK KLQVDPQLNQ NYTFESFIEG DCNRLARSAG YAVAAKPGGT SFNPLMIYGG
     VGLGKTHLAQ AIGNEIKRTL PDKLVLYVSC EKFTQQFVDA LKHNNINDFV NFYQAIDVLI
     MDDVHNFAGK EKTQDFFFHI FNHLHQSGKQ LIITSDKAPK DLAGLEERLL SRFKWGLSAD
     LQIPDLETRM AILKTKIYQD GIDLPYEVIE YVAHNIDNNV RELEGAMVSL LAQSTLNRKE
     IDLNLAKSML KNFIKNSTKE ISMEYIQSLV CEYFEVPIEM VKSQTRKREI VQARQISMYL
     AKAHTKSSLK SIGNFFGGRD HSTVIYACQT VEDLIDTDKK FKGYVADIQK KLKMS
//
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