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Database: UniProt
Entry: A0A402B2Z4_9CHLR
LinkDB: A0A402B2Z4_9CHLR
Original site: A0A402B2Z4_9CHLR 
ID   A0A402B2Z4_9CHLR        Unreviewed;       878 AA.
AC   A0A402B2Z4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=KDA_11770 {ECO:0000313|EMBL:GCE25693.1};
OS   Dictyobacter alpinus.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Dictyobacteraceae; Dictyobacter.
OX   NCBI_TaxID=2014873 {ECO:0000313|EMBL:GCE25693.1, ECO:0000313|Proteomes:UP000287171};
RN   [1] {ECO:0000313|Proteomes:UP000287171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Uno16 {ECO:0000313|Proteomes:UP000287171};
RA   Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA   Yabe S.;
RT   "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT   sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT   of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT   from Tengu-no-mugimeshi.";
RL   Submitted (DEC-2018) 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:GCE25693.1}.
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DR   EMBL; BIFT01000001; GCE25693.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A402B2Z4; -.
DR   OrthoDB; 9814968at2; -.
DR   Proteomes; UP000287171; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR018764; Anti-sigma_K_RskA.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
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   Pfam; PF10099; RskA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287171};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        515..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..291
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          371..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..860
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   878 AA;  94389 MW;  DFFA07E0F7D271EE CRC64;
     MSTSPRRIGQ YELLQQIGNG HVGEVWKAHD LAQRRDVAVK ILHNDLQADP NFLNRLTNGG
     KAITNLRHDN LVSVYDARVS RPNEARETTT FIVMDYIEGY TISDYLKATA QRGIFPATTD
     IVYLFSCLGA VVDYIHQQGI AHGDIKPSNI LLNKQQRTRF NAGEPMLTDV GITQIAGNDS
     YLGAPHYLSP EQAQGQSAKK ESDIYALGII LYELCTGATP FRGDNSFAVI SQHINTLPTP
     PTLLNANIPP DLAQVILRAL SKDPGARFSE GAQFAYAIAE ACSVQPTHPA VRQIATRSQQ
     AQTSSNPAQN NQQSILGVSQ PLTPASPVFM RPLIDMATRQ QSQAGQEQPI SLNANPNVSA
     AAVFPNSGPL SSVTIQKNPG PASLPSTAPA SGFPQSGPAS VPPSGATSGP LSGASGKQFQ
     LRQTSLTRIP VVGPDKPGLQ FSLPSTPSSP DLSATQQSQV RPDYVQAEPV RPYPQQPDPA
     AYRAYQQQAA PQIPQTPPPL AVPPPTRPAV YKNKYFILIA ALVLIAVIAA SIGLSNALKP
     NDKAGQPAPA VTTKNPLPTP QGPGIVFFQD DALGRNDQLR ITMKDIPDPA QGKVYYAWLQ
     TNTQKFVPLG AMQAQNKQID FMYAGDANHT NLINYTSGIQ ITLEDTGNNP TTPGKKVVYR
     AAFAQATLPE IQNILDSTPG LPKGQSAVSN MFETIKSLND KAASIVDSLD QTKDYGLVKR
     QATRIIELID GSNYARSSGD LPNTLPGQIK TPIGLLSSPN QPGYIDILDK HLDALKANAG
     NNANLQMRIQ NAKAGLTDLR QWLQKMRDND VQLLKATNLT DAKNHAAALQ LKQLADYSYK
     GRTIPPDTSP KSTPGSAGAS QTYVETQYMA ALDLTAVK
//
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