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Database: UniProt
Entry: Y1085_BIFLS
LinkDB: Y1085_BIFLS
Original site: Y1085_BIFLS 
ID   Y1085_BIFLS             Reviewed;         328 AA.
AC   B7GQU5; E8MJH0;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Nucleotide-binding protein Blon_1085/BLIJ_1109 {ECO:0000255|HAMAP-Rule:MF_00636};
GN   OrderedLocusNames=Blon_1085, BLIJ_1109;
OS   Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS   1222 / NCTC 11817 / S12).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=391904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA   Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA   Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA   Richardson P.M., Mills D.A.;
RT   "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT   adaptations for milk utilization within the infant microbiome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=21270894; DOI=10.1038/nature09646;
RA   Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA   Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA   Morita H., Hattori M., Ohno H.;
RT   "Bifidobacteria can protect from enteropathogenic infection through
RT   production of acetate.";
RL   Nature 469:543-547(2011).
CC   -!- FUNCTION: Displays ATPase and GTPase activities. {ECO:0000255|HAMAP-
CC       Rule:MF_00636}.
CC   -!- SIMILARITY: Belongs to the RapZ-like family. {ECO:0000255|HAMAP-
CC       Rule:MF_00636}.
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DR   EMBL; CP001095; ACJ52175.1; -; Genomic_DNA.
DR   EMBL; AP010889; BAJ68697.1; -; Genomic_DNA.
DR   RefSeq; WP_012577434.1; NZ_JDTT01000017.1.
DR   AlphaFoldDB; B7GQU5; -.
DR   SMR; B7GQU5; -.
DR   KEGG; bln:Blon_1085; -.
DR   KEGG; blon:BLIJ_1109; -.
DR   PATRIC; fig|391904.8.peg.1108; -.
DR   HOGENOM; CLU_059558_0_0_11; -.
DR   Proteomes; UP000001360; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00636; RapZ_like; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005337; RapZ-like.
DR   PANTHER; PTHR30448:SF0; RNASE ADAPTER PROTEIN RAPZ; 1.
DR   PANTHER; PTHR30448; UNCHARACTERIZED; 1.
DR   Pfam; PF03668; ATP_bind_2; 1.
DR   PIRSF; PIRSF005052; P-loopkin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding; GTP-binding; Nucleotide-binding.
FT   CHAIN           1..328
FT                   /note="Nucleotide-binding protein Blon_1085/BLIJ_1109"
FT                   /id="PRO_0000383219"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
FT   BINDING         101..104
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
SQ   SEQUENCE   328 AA;  35889 MW;  8DF80E844314BE59 CRC64;
     MSQQTTIRDT GEAAATNAPA NSATSTSTPD NQPTPLDAFE VLLITGMSGA GRSHAADCVE
     DMGWYVVDNL PPKLLIPLVD MMTTSGSGSG SGVHKLAAVI DVRSSYFDEL AAVLGHLDDL
     GVKTHILFLD ASNEVLIKRY ESVRRPHPLQ HGNRLIDGIL EERHLLEDLK ERADWVIDTS
     SLSIHQLSTK LYETMLGSGP TTVAVHIFSF GFKYGMPIDA DFVADVRFLP NPFWVPNLRE
     LTGHDKPVAD YVLSSKGAKE FLDAYEKAIE IALEGYAQED KHYVTIAVGC TGGQHRSVAM
     SEELARRLRA HGLNVTVSAR EQHKRHSS
//
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