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Database: UniProt
Entry: A0A0L8F1G3_9CLOT
LinkDB: A0A0L8F1G3_9CLOT
Original site: A0A0L8F1G3_9CLOT 
ID   A0A0L8F1G3_9CLOT        Unreviewed;       449 AA.
AC   A0A0L8F1G3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   05-JUL-2017, entry version 15.
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=AGR56_14340 {ECO:0000313|EMBL:KOF57527.1};
OS   Clostridium sp. DMHC 10.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=747377 {ECO:0000313|EMBL:KOF57527.1, ECO:0000313|Proteomes:UP000037118};
RN   [1] {ECO:0000313|Proteomes:UP000037118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DMHC 10 {ECO:0000313|Proteomes:UP000037118};
RA   Pore S.D., Kamalaskar L.B., Kapse N.G., Ranade D.R., Shouche Y.,
RA   Dhakephalkar P.K.;
RT   "Draft genome of biohydrogen producing Clostridium sp. DMHC 10
RT   isolated from sludge of distillery waste treatment plant.";
RL   Submitted (JUL-2015) 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}.
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:KOF57527.1}.
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DR   EMBL; LGVB01000015; KOF57527.1; -; Genomic_DNA.
DR   RefSeq; WP_053242847.1; NZ_LGVB01000015.1.
DR   EnsemblBacteria; KOF57527; KOF57527; AGR56_14340.
DR   PATRIC; fig|747377.3.peg.3410; -.
DR   Proteomes; UP000037118; 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; 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:UP000037118};
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:UP000037118}.
FT   DOMAIN      144    272       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      356    425       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     152    159       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   449 AA;  51571 MW;  096686E7B32BD22F CRC64;
     MGPQLKELWE KTLKIIKGEL TEVSFNTWIK SITPISISKD IIRFGVPNQF TKEILENRYK
     DLIINSLKII TTKKYDLIFS VVSEETIDIE ENNENIKSKD SSNNSEDTST MLNPKYKFDS
     FVIGNSNRFA HAACLAVAEA PAKAYNPLFI YGGVGLGKTH LMHAIGHYIL ENNPKAKVVY
     VSSEKFTNEL VNSIKDDKNV EFRTKYRNVD VLLIDDVQFI AGKERTQEEF FHTFNELHEN
     NKQIILSSDR PPKEIPTLED RLRSRFEWGL IADIQPPDFE TRIAILKKKA DVEKLDIPNE
     VMVYIATNIK SNIRELEGAL IRIVAFSSLT NKEISIDLAS EALKDIISNK QNKQITIELI
     QDVVASYFNI KIDDFKSSRR TRNITYPRQI AMYLCRKLTD MSLPRIGEEF GGRDHTTVIH
     AYEKISGALK DDEELKHTIK EITKRFSQK
//
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