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Database: UniProt
Entry: C6XTL9_PEDHD
LinkDB: C6XTL9_PEDHD
Original site: C6XTL9_PEDHD 
ID   C6XTL9_PEDHD            Unreviewed;       476 AA.
AC   C6XTL9;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   23-MAY-2018, entry version 73.
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   OrderedLocusNames=Phep_3606 {ECO:0000313|EMBL:ACU05797.1};
OS   Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM
OS   7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3).
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU05797.1, ECO:0000313|Proteomes:UP000000852};
RN   [1] {ECO:0000313|EMBL:ACU05797.1, ECO:0000313|Proteomes:UP000000852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 /
RC   NCIMB 9290 / NRRL B-14731 / HIM 762-3
RC   {ECO:0000313|Proteomes:UP000000852};
RX   PubMed=21304637; DOI=10.4056/sigs.22138;
RA   Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A.,
RA   Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA   Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Saunders E., Chertkov O., Brettin T., Goker M.,
RA   Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of Pedobacter heparinus type strain (HIM
RT   762-3).";
RL   Stand. Genomic Sci. 1:54-62(2009).
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:SAAS00747961}.
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; CP001681; ACU05797.1; -; Genomic_DNA.
DR   RefSeq; WP_015809406.1; NZ_AQGK01000003.1.
DR   STRING; 485917.Phep_3606; -.
DR   EnsemblBacteria; ACU05797; ACU05797; Phep_3606.
DR   KEGG; phe:Phep_3606; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   BioCyc; PHEP485917:G1GFH-3617-MONOMER; -.
DR   Proteomes; UP000000852; Chromosome.
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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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:UP000000852};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00747973};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00748008};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000852}.
FT   DOMAIN      172    302       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      383    452       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     180    187       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   476 AA;  53893 MW;  99157391B59067AF CRC64;
     MEKTCIEVWK NCLQIIKDNI PTQSFKTWFE PISALKLEGN VLTIQVPSLF FYEWLEEHYV
     GLLRKTVKKQ LGDEGRLEYN IVVDKSSNSG SPYTTNMPSN GNGADAKKQS MPIPVSINKD
     IKNPFIIPGL KKLNVDPQLN ANYTFENYIE GDCNRLARSA GYAVAAKPGG TSFNPLMIYG
     GVGLGKTHLA QAIGNEIKRN MPDKLVIYVS CEKFCQQFVD SLKNNTINDF VNFYQAMDVI
     IMDDVHNFAG KEKTQDIFFH IFNHLHQSGK QVILSSDKAP KDLAGLEERL LSRFKWGLSA
     DLQVPDLETR IAILRKKMYA DGIELPAEVV EYVAHNIDNN VRELEGAMVS LLAQSTLNKK
     DIDLALAKQM LKNFIKNTSK EISMEYIQKL VCEYFEVPVD MVKSQTRKRE IVQARQISMY
     LSKSHTKSSL KTIGAFFGGR DHSTVIYACQ TVEDLIDTDK KFKGYVHDIQ KKLKMS
//
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