ID   Q7UMB3_RHOBA            Unreviewed;       510 AA.
AC   Q7UMB3;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=RB8929 {ECO:0000313|EMBL:CAD76004.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD76004.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD76004.1, 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; BX294148; CAD76004.1; -; Genomic_DNA.
DR   RefSeq; NP_868627.1; NC_005027.1.
DR   AlphaFoldDB; Q7UMB3; -.
DR   STRING; 243090.RB8929; -.
DR   EnsemblBacteria; CAD76004; CAD76004; RB8929.
DR   KEGG; rba:RB8929; -.
DR   PATRIC; fig|243090.15.peg.4286; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_534068_0_0_0; -.
DR   InParanoid; Q7UMB3; -.
DR   OrthoDB; 6111975at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 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:CAD76004.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:CAD76004.1};
KW   Transferase {ECO:0000313|EMBL:CAD76004.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        485..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          77..343
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          354..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..393
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   510 AA;  55270 MW;  1C831FCAF800C3C1 CRC64;
     MASITSERFV EMVARSNLVD EATQERFLKK VREKCEGNLP ASSKKLALAY KKAGLLTDWH
     IEKLFTGKYK GFFLGKYKLL GHIGSGGMSS VYLAEHIGLG DKRAIKVLPK KRVNDASYLA
     RFKLEAKAIA SLNHPNIVLA HDIDNDGDVH YIVMEYVDGV DLQVLVRRDG PLDFSTAAEL
     ISQAARGLAH AHNRGVVHRD VKPANLLIDS DGRVRLLDMG LALVSKTGDD ESLTVANNEN
     VLGTADYLAP EQALNSHTVD HRVDIYGLGC TLYFLLTGRP PFAEGTLAQR IAKHQNEMPK
     AIRELRPECP GELEGIVVKM IQKDPRYRYQ NATDVAEVLE KFAAAVPKGE AIRVGLGEGP
     DEDSSLSSMD FDSSSGSMVT QSNQDTLTNK NDDTLASSRS KLIREQNQAA SESGRLVKVG
     SMGTPADMLE GSFLDLEVES GYKGPTARAP SSGSRRGVGS GIDRGKPSDT RTQLADNRSK
     GIDPVLLGTV VTSLFVAALA LGYFLAKVTS
//