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Database: UniProt
Entry: R6G5H7_9CLOT
LinkDB: R6G5H7_9CLOT
Original site: R6G5H7_9CLOT 
ID   R6G5H7_9CLOT            Unreviewed;       454 AA.
AC   R6G5H7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   25-OCT-2017, entry version 30.
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=BN542_01975 {ECO:0000313|EMBL:CDB16794.1};
OS   Clostridium sp. CAG:221.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium; environmental samples.
OX   NCBI_TaxID=1262780 {ECO:0000313|EMBL:CDB16794.1, ECO:0000313|Proteomes:UP000018176};
RN   [1] {ECO:0000313|EMBL:CDB16794.1, ECO:0000313|Proteomes:UP000018176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:221 {ECO:0000313|Proteomes:UP000018176};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) 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: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:CDB16794.1}.
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DR   EMBL; CBDC010000115; CDB16794.1; -; Genomic_DNA.
DR   Proteomes; UP000018176; 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; IPR024633; DnaA_N_dom.
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:UP000018176};
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:UP000018176}.
FT   DOMAIN      149    277       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      361    430       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     157    164       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   454 AA;  51725 MW;  24B0A15C7A0B0D63 CRC64;
     METDLKKLWE NTLNIIKGEM SEVSFNTWIK SCEPISISSN TIKISVPNVF TQDILEKRYK
     DLVINSIYSA CSKQYNVEFL TESEIQEANS DKPTDSSEQN HKDSMSITVS DEMSSTLNPK
     YTFDSFVIGN SNRFAHAASL AVAESPAKAY NPLFIYGGVG LGKTHLMHAI GHYILQGNPN
     AKVVYVSSEK FTNELINSIK DDKNEEFRTK YRSVDVLLID DIQFIAGKER TQEEFFHTFN
     TLHDANKQII LSSDRPPKEI PTLEDRLRSR FEWGLIADIQ APDFETRMAI LKKKADVEKL
     NVPNEVMVYI ATKIKSNIRE LEGALIRIVA YSSLTNREIT VDLATEALKD IISNKQNKNI
     TIDLIQDVIA AYFNLRVEDL KSQRRTRNIA YPRQIAMYLS RKLTDMSLPK IGEEFGGRDH
     TTVIHAYEKI SEGLKSDESL QRTIDDITKK ITQK
//
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