ID   A0A142XB90_9BACT        Unreviewed;      1432 AA.
AC   A0A142XB90;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Serine/threonine-protein kinase PknL {ECO:0000313|EMBL:AMV24235.1};
DE            EC=2.7.11.1 {ECO:0000313|EMBL:AMV24235.1};
GN   Name=pknL_1 {ECO:0000313|EMBL:AMV24235.1};
GN   ORFNames=VT84_07550 {ECO:0000313|EMBL:AMV24235.1};
OS   Gemmata sp. SH-PL17.
OC   Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC   Gemmata.
OX   NCBI_TaxID=1630693 {ECO:0000313|EMBL:AMV24235.1, ECO:0000313|Proteomes:UP000076098};
RN   [1] {ECO:0000313|EMBL:AMV24235.1, ECO:0000313|Proteomes:UP000076098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH-PL17 {ECO:0000313|EMBL:AMV24235.1,
RC   ECO:0000313|Proteomes:UP000076098};
RA   van der Voort M., Raaijmakers J.M.;
RT   "Genome minning of novel planctomycete species.";
RL   Submitted (APR-2015) 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};
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DR   EMBL; CP011271; AMV24235.1; -; Genomic_DNA.
DR   STRING; 1630693.VT84_07550; -.
DR   KEGG; ges:VT84_07550; -.
DR   OrthoDB; 272334at2; -.
DR   Proteomes; UP000076098; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR025139; DUF4062.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR005532; SUMF_dom.
DR   InterPro; IPR042095; SUMF_sf.
DR   PANTHER; PTHR23150:SF19; FORMYLGLYCINE-GENERATING ENZYME; 1.
DR   PANTHER; PTHR23150; SULFATASE MODIFYING FACTOR 1, 2; 1.
DR   Pfam; PF13271; DUF4062; 1.
DR   Pfam; PF03781; FGE-sulfatase; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 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   Kinase {ECO:0000313|EMBL:AMV24235.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076098};
KW   Transferase {ECO:0000313|EMBL:AMV24235.1}.
FT   DOMAIN          124..410
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   1432 AA;  160165 MW;  D9E30A8BAE25FA6E CRC64;
     MPGPQDSPSA GGSGRSPDPL LAQMVFEATW DLLTRWQNGQ PIPAEAYRAD FGDALFSRQD
     VGPRLVAAQM RARFELFPAL ATGPTLRSAD PLLDLFGCRR PQSAPYPYFA PPRAGGEIGW
     FETFRVIREV GRGGLGIVFR AFNTRAVVGK DRPRALKLLI PEGDLTKSRQ RLEAEAASLW
     AIRHDHVVAF YDAKTVTHPD AGEIDYLEME YVYGPSLEDL VVHFQRDGCP VPLRLAVELI
     RQAAAGLDGI HTHTQEFIHR DLKPSNLLLE WRPDSPPNGS PWRVRLCDFG LVRAAERPRI
     TSETSIVGTR VYMAPEQLRS VPRRPVSTKS DIFALGVILY ELVVGRHPFL ADTVTQTDEN
     IFRLRYTHPR EANRSVDIPE SLDTLIRAML AEHPTKRPDA VTVRDRLAAI ADPGAGAPPN
     RERAPRAVRR PADSAAALMK VYVSSVAKEL IPFRRAVVEA IRAAPDRYVV FPPQEYAEEF
     AFPVEECQKW IAQCHVYVGL FGFDYGPILK EDSVSLLERE YRASLGWKLT PLLFMSERPH
     RKLHSSAEWQ ALGASPIHAL RSELETARAV LFSDSREALA AQVLAALSTL LLPEAVGSSP
     GSSGSSDTDW SRRALENYRK KVCAGFTFYN EAHPDASEND PSRKELPFLR SQQLFTLKPG
     VDAKEALHPE RFRAARLASD DRSGEPPTPD AQYWEELDRE ALIASLTGDA KGHRIALTTD
     AGLGKTRNLA WLEHECQSRG PGWVFSLLAG ETLPLHQLVP KRLAERVLAA NNTNLDELQV
     AAILEAARTD GAITLIVDGL DQTKTVGWLK DLLDPTAGWD RCHVVVAGRP FALESHWEDL
     FAAPNWQYVQ IGELNRKQQE QLLGERRFGA VPEEARSILS TPRVLECIRG IDEKELPTLR
     TVADVYWKAV RYMLVRALRP HPGGKIDRED ERRYLQILGA LAFAMYAETE SDGNGNLRPN
     LDRILAGDDL LDFLYGPRDG KRSVLERLQP IIPNYDKERF KNDLKTLSAL NAAVSHGWLD
     SDGLGTNAPP LLWRNASLQE FFAAYWVCRW DASDAELLGG WAVDPHSGKN RAFYWLWRYA
     SEMPEEVIWP NRKAPPMDAW VAAMTPLYVA PPDKDGLPIR SSEFLYRSWL RPGAEGFVDP
     MAHSKKGREA RATFLTEFPK ILEEADSERQ RIALELSDAF IPLIGQPGAS GSFLMGSAGD
     DKLALADEKP RHEVTLSAFA LHRYCVSNVA FELYDPWHRN VRWEHKKQHP LVAANGPSAD
     DRCPVVNVSW YDAWCFARWL GSVEIGDRRY RVGLPSEAQW EYACRAGTGT LYWSGNEEAD
     LASVARYGRN SGGHTHAVDE DRSRNPWGVF QIHGNVWEWC ADWYLASFYS SKEGSFQDPV
     NFAPASARVL RGGSWYGVGR YCRSAARGKT EPDDRHQSIG FRLAAVPVVG AE
//