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Database: UniProt
Entry: D1A6D2_THECD
LinkDB: D1A6D2_THECD
Original site: D1A6D2_THECD 
ID   D1A6D2_THECD            Unreviewed;       557 AA.
AC   D1A6D2;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=Tcur_4709 {ECO:0000313|EMBL:ACZ00231.1};
OS   Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS   9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Thermomonospora.
OX   NCBI_TaxID=471852 {ECO:0000313|EMBL:ACZ00231.1, ECO:0000313|Proteomes:UP000001918};
RN   [1] {ECO:0000313|EMBL:ACZ00231.1, ECO:0000313|Proteomes:UP000001918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC   NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX   PubMed=21475583; DOI=10.4056/sigs.1453580;
RA   Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL   Stand. Genomic Sci. 1:13-22(2011).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP001738; ACZ00231.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1A6D2; -.
DR   STRING; 471852.Tcur_4709; -.
DR   KEGG; tcu:Tcur_4709; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_489094_0_0_11; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000001918; Chromosome.
DR   GO; GO:0005886; C:plasma 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-KW.
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; IPR025199; FtsK_4TM.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF13491; FtsK_4TM; 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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000313|EMBL:ACZ00231.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001918};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ACZ00231.1};
KW   Transferase {ECO:0000313|EMBL:ACZ00231.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        381..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        412..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        448..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        505..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..271
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          275..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..331
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   557 AA;  58732 MW;  1074E07AB1B53A64 CRC64;
     MEPGALLDGK YRLVRRLGQG GMGEVWAAED LSLNRQVAVK IVLSNLGTNQ EVIARLRREA
     QAAASLQHPG ITVVHAMGEH EGHPFVVMEL LNGRDFMAIL EANPNGIPVA HAVSLAAQVA
     DALAYAHRNG VVHRDIKPAN LMELTDGRVK ICDFGIARFA DAAPDLTPMG MILGTPPYTA
     PEQYRGGPVD GRSDLYSFGC TLYALLTGRP PFTGPSIAAF MNQHLHEPPP RPSELRPDIP
     AELENLVLGM LAKDPADRPS MEEVLARLNA LNSPAPAPPA APAATLPFAP DAPPPFPQAD
     PAVLPPVGPP PAAVHQAPLS PLPPPSPPSP AAQALNEAVN RLRSSRAPVR AWRAVASAAG
     WLLRAPGGAG RDLDPALRRD GLGLVLLIAA LTCGGLLWSQ TELTVTTKTA DFLRGVFGVC
     AYVLPVLLFL LAARIFRSPE RREANARIVS GSVVTSLAVL GVIHISAETP NPLKTDDLEP
     IRDAGGVVGW MVGAPLEAAL TPWGAIPLLL VLGGLGLLIA TATPLNELPE RIGRLLGLLT
     SDRDRTPEGQ RQGPANS
//
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