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Database: UniProt
Entry: A0A1Y4ERL6_9FIRM
LinkDB: A0A1Y4ERL6_9FIRM
Original site: A0A1Y4ERL6_9FIRM 
ID   A0A1Y4ERL6_9FIRM        Unreviewed;       439 AA.
AC   A0A1Y4ERL6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=B5F54_14395 {ECO:0000313|EMBL:OUO72649.1};
OS   Anaeromassilibacillus sp. An250.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Anaeromassilibacillus.
OX   NCBI_TaxID=1965604 {ECO:0000313|EMBL:OUO72649.1, ECO:0000313|Proteomes:UP000195568};
RN   [1] {ECO:0000313|EMBL:OUO72649.1, ECO:0000313|Proteomes:UP000195568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An250 {ECO:0000313|EMBL:OUO72649.1,
RC   ECO:0000313|Proteomes:UP000195568};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T.,
RA   Cizek A., Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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:OUO72649.1}.
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DR   EMBL; NFJK01000019; OUO72649.1; -; Genomic_DNA.
DR   Proteomes; UP000195568; 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   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:SAAS00756129};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000195568};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195568}.
FT   DOMAIN      134    262       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      346    415       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     142    149       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      296    316       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   439 AA;  49856 MW;  0071B7B4241A906D CRC64;
     MESFTEAWSF ICEYCKKHIT EVAYTTWISR IEPVSLDFAK GIALLKAPNE FHRQTLNRCY
     MDLLNDAVAE IFGPGIQVQI CVPEDVPSAE KEEEEDASSQ NDDYEFTFDT FIVGPSNKFA
     HAASMAVATK PATLYNPLFI YGNSGLGKTH LLYAICNEIA RRHPEMNIVY IKGDEFTNEL
     IEAIRHGTTA EFHQRYRKAD VFLVDDIQFI AGKESTQEEF FHTFNTLYEA KKQIVLTSDR
     PPKDIATLEE RLLTRFEWGL TADIQPPDFE TRIAIIKRKA ELLGIDLPNN VIEYIANRLK
     NNIRQLEGTV KKMKAYYLLN GDALNLSTAQ MAVSDIINNE QPVPVTVEKI IEEVARTYGT
     SPEDIRSSKR SANISNARQV AMYVVREITQ MPMTSIGEEF GGRDHSTVVY AIQQVEKGMA
     RDPKTKGTVE DIIKNIRDR
//
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