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Database: UniProt
Entry: D4YTT6_9LACO
LinkDB: D4YTT6_9LACO
Original site: D4YTT6_9LACO 
ID   D4YTT6_9LACO            Unreviewed;       459 AA.
AC   D4YTT6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   30-AUG-2017, entry version 48.
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   ECO:0000313|EMBL:EFG55445.1};
GN   ORFNames=HMPREF0493_0947 {ECO:0000313|EMBL:EFG55445.1};
OS   Lactobacillus amylolyticus DSM 11664.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=585524 {ECO:0000313|EMBL:EFG55445.1, ECO:0000313|Proteomes:UP000004069};
RN   [1] {ECO:0000313|EMBL:EFG55445.1, ECO:0000313|Proteomes:UP000004069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11664 {ECO:0000313|EMBL:EFG55445.1,
RC   ECO:0000313|Proteomes:UP000004069};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z.,
RA   Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L.,
RA   Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
RA   Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
RA   San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
RA   Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
RA   Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (APR-2010) 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:EFG55445.1}.
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DR   EMBL; ADNY01000035; EFG55445.1; -; Genomic_DNA.
DR   ProteinModelPortal; D4YTT6; -.
DR   STRING; 585524.HMPREF0493_0947; -.
DR   EnsemblBacteria; EFG55445; EFG55445; HMPREF0493_0947.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000004069; 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:UP000004069};
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}.
FT   DOMAIN      155    284       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      367    436       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     163    170       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   459 AA;  52576 MW;  BD2439E4D395C6CC CRC64;
     MGEFILFDID KFWQHFNDEM RERFNEVAYN AWFKNTKPLS YDKNSHELKI AVQNPVSKGY
     WEKNLSSQLI QSAYGYAGIE ILPTFQIEGD TGPERIVTPE PRHEIQQNIP QPRQDEFAKD
     LKLNDKYTFD NFVQGEGNKL AAGAALAVAD SPGSFYNPLF IFGGVGLGKT HLMQAIGHQM
     LAERPNAKIV YIQSETFVND FINSIKNKTQ DQFREKYRTC DLLLVDDIQF FAKKEGIQEE
     FFHTFETLYN DQKQIVMTSD RLPTEIPDLS ERLVSRFTWG LQVEITPPDL ETRIAILRKK
     AEADGLTIDD NTLDYIASQV DTNIRELEGA LVKVEAHATI EKEDINVNLA RDALADLKLV
     QKNRGLQISK IQEVVANYFQ TSIAELKGKK RVRQIVVPRQ VAMYLSRELT DASLPKIGQE
     FGGKDHTTVM HAYEKIQQQI KTDADIKSAI FDLRQMLDR
//
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