ID   Q7UN41_RHOBA            Unreviewed;       937 AA.
AC   Q7UN41;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 117.
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=pkn {ECO:0000313|EMBL:CAD75578.1};
GN   OrderedLocusNames=RB7798 {ECO:0000313|EMBL:CAD75578.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD75578.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD75578.1, 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; BX294146; CAD75578.1; -; Genomic_DNA.
DR   RefSeq; NP_868031.1; NC_005027.1.
DR   AlphaFoldDB; Q7UN41; -.
DR   STRING; 243090.RB7798; -.
DR   EnsemblBacteria; CAD75578; CAD75578; RB7798.
DR   KEGG; rba:RB7798; -.
DR   PATRIC; fig|243090.15.peg.3763; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_312806_0_0_0; -.
DR   InParanoid; Q7UN41; -.
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; 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   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 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.
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:CAD75578.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW   Transferase {ECO:0000313|EMBL:CAD75578.1}.
FT   DOMAIN          113..383
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   937 AA;  103176 MW;  A3DC68A913C6AD23 CRC64;
     MRGQPIDPSH RKPVMIATST DCLSVEELNR LLDGQLSSDE FDSASKHVDE CEQCQSRIPD
     KWDALSSVAK AGTEEDSVLA ESACQFAVAR LMTAHIASSH VSADLPIDQI GPYEILGKLG
     QGGMGMVCLA RHNRLKRQCA IKLLPPHRVM EPGWLDRFDR EMTTIAALEH PGIVRATDAG
     THSGWHYLVM EHLDGMDVGK IAYRLGSLPV ADACEIARQS AVALMHVHET GLIHRDVKPS
     NLMLTRDGTV KLLDLGLVLA GDDPLATDDR LTTVGHLMGT LPAMSPEQLL DSRKVQPASD
     IYSLGATLYR LISGRWPHAN EGGLAARVLA ITSESNRSTP PPLSRLEPSV ESELQTFVDQ
     MMHRQPDQRP SGSVVAERLA TWSGDANLKA LLKRAEATPV SDAPITPSFS LATKPASPPP
     GGGKHNWTAW FGPLGWFAAA ILLATVVIQI KTDKGLVTVT TDGKDTQVAV EKNDEDSTED
     TVLPSAEKSL AIGLESTDGE KIYLGENLDY WLVVFRREQQ MERIGQAMRA VELLSRNTPK
     REEAARVTLE LANEYGTQII DDTPDQNGGG FGGQSPPNQR FMGYLTQTFD NYLPTPGLRP
     LGETLVDGNE KAKIAAITLL NQYLSGVQGN TFYAEREESV TEFFSQSGAT VDGRSKTETL
     LQQLGKASDD LRMSASKASH EDRSMNNAAG EAYYARLSAW SVAMRIVKMT GPHTATPNWI
     AEYVQEQVDE AVAVYEQREI DPDTRQTKWD YTNPNAAYGF SMGGFGGGSQ MITSPTAPDW
     LLSRELIISA IEMQREGRLD LPIQFAAETL AHPSFNWYPL EGGTLDDVVQ TLTAIDPKAP
     FLIAFHLDRS FQEMDRQYQA SQNAEWLRPL TFLRQRLQEG LASVYTTHVE QPKQAHDRLG
     RLVNSLPKLS SLQLTTDHDK DFWLSMLNDL KQRSESE
//