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Database: UniProt
Entry: B6XTR5_9BIFI
LinkDB: B6XTR5_9BIFI
Original site: B6XTR5_9BIFI 
ID   B6XTR5_9BIFI            Unreviewed;       734 AA.
AC   B6XTR5;
DT   20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2009, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=BIFCAT_00543 {ECO:0000313|EMBL:EEB21585.1};
OS   Bifidobacterium catenulatum DSM 16992 = JCM 1194 = LMG 11043.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=566552 {ECO:0000313|EMBL:EEB21585.1, ECO:0000313|Proteomes:UP000003882};
RN   [1] {ECO:0000313|EMBL:EEB21585.1, ECO:0000313|Proteomes:UP000003882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16992 {ECO:0000313|EMBL:EEB21585.1,
RC   ECO:0000313|Proteomes:UP000003882};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Bifidobacterium catenulatum (DSM 16992).";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB21585.1, ECO:0000313|Proteomes:UP000003882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16992 {ECO:0000313|EMBL:EEB21585.1,
RC   ECO:0000313|Proteomes:UP000003882};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEB21585.1}.
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DR   EMBL; ABXY01000011; EEB21585.1; -; Genomic_DNA.
DR   RefSeq; WP_003834445.1; NZ_JDTP01000027.1.
DR   AlphaFoldDB; B6XTR5; -.
DR   GeneID; 45583024; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   Proteomes; UP000003882; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 3.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR45832:SF24; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 1.
DR   Pfam; PF03793; PASTA; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EEB21585.1};
KW   Transferase {ECO:0000313|EMBL:EEB21585.1}.
FT   DOMAIN          17..283
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          591..657
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          658..731
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          307..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   734 AA;  79009 MW;  76889318C1969F60 CRC64;
     MSEAPHAPEG QVIEGRYRVV SRIADGGMAT VYQAVDERLG RTVAIKIMHT QLAQGPHRDQ
     FVERFHREAR SAAAIANPHI VQVYDTGEFD GLDYLVMEYV HGVNLRYEMN QQGTFSVRET
     LRIIGETLDG LASAHRAGVV HRDIKPENIL LNDRGHVQIT DFGLAKTVSQ ATLSSTGILL
     GTAAYLAPEM IERNQATPQG DLYSVGIMAW EMLAGKVPFT SNNPVTLVFK HVHEDVPSIV
     TVCEGINANV AAFIAHLTAR AVEARPADAS AALAELQRLQ SILAVSDWQY QLPAANVNIS
     PNTTQAEDAA APMNEGNPAP PTPPAPPTQQ FDDRTRKLDR VKPNMTTVMP VQQQNVDPEA
     TTRFSLPLDG DVNTADGSTR PQSPAMQNGD YGNAGKDESS KRHRTPLIVA GVAAFLLTCG
     AGGWAWWCYQ GPGSYWTMPQ PDGMSCSDSV ACPITGVKWS DYESLLKVSD IEYEVSEKYS
     DSITEGDIIS TDPANVGDRG SKRRGQKVKV VVSKGVRQAT VPADILDATS ASGKDPINAL
     KKAGFDNVEQ TTASDDTYSM EVPQGALLSL SVDPGATLPH NTTITVTVSQ GPKPVTMPNI
     VGKTKDEAQQ TMDDLKLTAN WTESFDDKIP QGQVISTSVS SGNTLHWGDS VDVVVSKGPE
     TITLPNYVGQ KASDAKAALE KLGFTVKVSS QLTLNASQDK KVASQDPVGG TEVRIRDENG
     TPTTITLKMY SSLF
//
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