ID   Q01ZY1_SOLUE            Unreviewed;       947 AA.
AC   Q01ZY1;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
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=Acid_3814 {ECO:0000313|EMBL:ABJ84784.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ84784.1};
RN   [1] {ECO:0000313|EMBL:ABJ84784.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ84784.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Janssen P.H., Kuske C.R., Richardson P.;
RT   "Complete sequence of Solibacter usitatus Ellin6076.";
RL   Submitted (OCT-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};
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DR   EMBL; CP000473; ABJ84784.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01ZY1; -.
DR   STRING; 234267.Acid_3814; -.
DR   KEGG; sus:Acid_3814; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_013589_0_0_0; -.
DR   InParanoid; Q01ZY1; -.
DR   OrthoDB; 105170at2; -.
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; 3.40.50.10610; ABC-type transport auxiliary lipoprotein component; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
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   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13431; TPR_17; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABJ84784.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABJ84784.1};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:ABJ84784.1}.
FT   DOMAIN          15..285
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          527..560
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   947 AA;  103603 MW;  708972201C4F2F27 CRC64;
     MGTQTPLAGQ TVGHYRIVGK LGSGGMGVVY KAEDILLHRF VALKFLPEHI VHDARALARF
     QREARAASAL NHSNICTIHE VTEYNHQPVI VMELLEGDTL RERIRGGALP LEEILNLAVQ
     ATDALDAAHE KGIVHRDVKP ANIFVSKRGH LKMLDFGLAK VDSPLASTET DAPTATIEER
     LTDTGSTMGT AWYMSPEQVR AKELDGRTDL FSFGVVLYEM ATGTLPFRGE SQGVVFDAIL
     NQTPVPPVRL NPDLPAELER IIAKCLEKDR NLRYQHASEI RSDLLRLKRD SDSHITVVVK
     HPSWITVKPG VLLAGAVVVV AAALGFYWYG HRAPRLTNRD TIVLADFVNT TGDAVFDGTL
     LQGLAIQLQQ SPFLSLVSEE RIHKTLKLMG QPADARLTPD LAREICQRTG GAAVLDGSIK
     SLGSQFVLGL RARNCGTGDV LDEEQAQAGK KEDVLNALSQ IASKFRTRVG ESLSTVKEHD
     TPLPEATTSS LDALKAYSSA RKVHLSLGGA PAMPLYRRAI EIDPGFAMAY ANLGHAYGEI
     GESDLSAEST RRAYQLRDRA SDAEKFYISV SYDFRVTGNL ENGLKTAELW AQTYPRDVNP
     FVFLSSILGI TGKNEKSVEA AAKAIELDPE FGFAYGMLTV NYLAFGRLEE AETTMRRAAD
     RKLDDIGFPF VRFDIAFLRG VKAGIDREVA LARGVPGLED LMADKEAFLM AYYGYLQQAR
     KQTQHASDLA QQASQKESSA LYQVGAAVRE SFYGNAAAAR KNAEAALELS RDREVVYGAA
     LALARSGDEP ASQLLAKDLE KRFGEDTSVR FSYLPVLRAV YAMNHGEPDK AIAVLQIASA
     QELSLPRTAI HAFFGALYPI YVRGEAYLKA HQSVQAAAEF QKIVDHRFLV LSDCIGALAH
     LELGRAYAMS GDLAKAKAAY NDFLTLWKDA DAEIPVLIQA KAEFAKL
//