ID   Q7UKJ3_RHOBA            Unreviewed;       766 AA.
AC   Q7UKJ3;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=pknB {ECO:0000313|EMBL:CAD76640.1};
GN   OrderedLocusNames=RB10119 {ECO:0000313|EMBL:CAD76640.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD76640.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD76640.1, ECO:0000313|Proteomes:UP000001025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC   {ECO:0000313|Proteomes:UP000001025};
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294150; CAD76640.1; -; Genomic_DNA.
DR   RefSeq; NP_869254.1; NC_005027.1.
DR   RefSeq; WP_011122624.1; NC_005027.1.
DR   AlphaFoldDB; Q7UKJ3; -.
DR   STRING; 243090.RB10119; -.
DR   EnsemblBacteria; CAD76640; CAD76640; RB10119.
DR   KEGG; rba:RB10119; -.
DR   PATRIC; fig|243090.15.peg.4882; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2358; Bacteria.
DR   HOGENOM; CLU_364417_0_0_0; -.
DR   InParanoid; Q7UKJ3; -.
DR   OrthoDB; 6111975at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR011852; TRAP_TAXI.
DR   NCBIfam; TIGR02122; TRAP_TAXI; 1.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF16868; NMT1_3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CAD76640.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW   Transferase {ECO:0000313|EMBL:CAD76640.1}.
FT   DOMAIN          154..416
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   766 AA;  82695 MW;  251B7CC08B3D7735 CRC64;
     MVEDVMAESN EDDLDEIFAL YLSACDTGEL TSRDDFLNQH PEHADQLREL MDAADLIGTF
     SMAGSDAKGT SGPWTEPITL PPDAEISDQA AQLASTASQI DVQTDMADTI GIGTALSADG
     LGEHSNVDPN LTLPMANRSQ GDSGPSLPFD LGDYQLLKVL GVGGMGVVYL AKQRELDRLV
     AVKMIRSGIL AGQDEVKRFY TEAKAAAKLK HPNIVAVHQF GRRAGHHFFS MQYVEGEDLQ
     KVLAKGPLPS RRAAEIVRDV AHAIHHAHSR GVLHRDLKPG NVLIDPSGQV HVTDFGLAKH
     TDADSSVTGS GAAVGTPHYM APEQALGHSD RVTHHSDIYS LGAILFAAIT SRPPIVGDTV
     MQTLLKVAHQ PPPTLRSVCP EAESDLEVIV AKCLEKQPKD RYKTAKNLAD DLNRFLCGQT
     IHARSRSRAR KVVDWFGQVP VVAAVTGRQT SGTPVGQRRF QNGILSASLI LPLLLFGGLV
     WQQRINNAMP TQIRIAGGLP GGLYNRVSEQ LSKTLQSQTS VPCEVIGTNG TWDNRERLIA
     GEFELAPIQA TAVNGETLRV VAPLFYEAVH VLIRDDSEID SVEDLSGQRI AVGPHGSGSR
     RAAEMVLESL GLSESVSPRV EMPWDTLQET NPKVSAEAAI ICIGVGSDLV TRMLAEQRWH
     LLPLPDGVSI ALQHPTLHAM TIATDAYAGS SIPPSGIHTV GTTAFLVCRD SAPDPLIEST
     LQALYEEPSI VGLIPARQAA EWQGLAFHRI SRRYYDDLEA RLANTQ
//