ID   A1A3W0_BIFAA            Unreviewed;       718 AA.
AC   A1A3W0;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Widely conserved protein with eukaryotic protein kinase domain {ECO:0000313|EMBL:BAF40393.1};
GN   OrderedLocusNames=BAD_1612 {ECO:0000313|EMBL:BAF40393.1};
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=367928 {ECO:0000313|EMBL:BAF40393.1, ECO:0000313|Proteomes:UP000008702};
RN   [1] {ECO:0000313|EMBL:BAF40393.1, ECO:0000313|Proteomes:UP000008702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a
RC   {ECO:0000313|Proteomes:UP000008702};
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) 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   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR   EMBL; AP009256; BAF40393.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1A3W0; -.
DR   STRING; 367928.BAD_1612; -.
DR   PaxDb; 1680-BADO_1726; -.
DR   KEGG; bad:BAD_1612; -.
DR   HOGENOM; CLU_000288_135_6_11; -.
DR   Proteomes; UP000008702; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:BAF40393.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008702};
KW   Transferase {ECO:0000313|EMBL:BAF40393.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        538..571
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        615..634
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        664..685
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          52..320
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   718 AA;  76405 MW;  D2C7EED844CB3FE0 CRC64;
     MSMIRFHQTS TCGTWRFPSL SIRVHNLHAK YDGSMSDLSA LNLEAGSLVG GYTLISRLGS
     GAMGSVWRVR DDGGHQYAMK ILRDSLSDDD SPQRQRDQLT ARERLRREAM ALQKVRHPGV
     CGIVDMELDD ALAFIVTELI EGKNLREDVR VNGRYVGDDL ERLARKLIEA VRAVHASGIV
     HRDIKPTNVM VSSTGPVLVD FGIAMGEGES HVTRTGLVMG TPGFIAPEII DGAESDEMTD
     WWSVASVLAF AATGEPVFGT KPMMTVLERA AAGSANLAGL PAGTMAAFRS ALNPDRTKRC
     TPDDLLQAIA VDALNPQAWV AADNGGAADG DTEAMPPFVE SPDNPRTLWR LQDDITGENA
     IGTRTMPRLS EATQAIGQPD VSATQVIGKQ VTSQSDASAT QVIAPVDDAE TRVLSDALPN
     VDSTRTMPQS QGTRAMPTGT QVMPQSMPST QMLPAQNAWN PAEAPTQVDP TIKPALQRIA
     MRQPPSVIPQ ATVAAAQQSP AMSFPPVPGM DGPNVAEAPN PADVKRGAML GRGMLPCALM
     AIPVAVCGLF SLWTAMAAAL LFACALATIG FNTEAQLERE GKRGGEKKSS DWLLRLAGLP
     WHIVKGFGVA IVRTLIMLAV AALGLSLTTV VLQLPYAVMD MWIFGLTIPM PTLLGGPLSE
     SGLAQAAFCA IGWLVAVAAP GAIVLRLGGG ALRKQPYLRH LSELPTQSQG NTEFPANR
//