ID   Q7UHE0_RHOBA            Unreviewed;       783 AA.
AC   Q7UHE0;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 115.
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:CAD78033.1};
GN   OrderedLocusNames=RB13265 {ECO:0000313|EMBL:CAD78033.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD78033.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD78033.1, 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; BX294156; CAD78033.1; -; Genomic_DNA.
DR   RefSeq; NP_870955.1; NC_005027.1.
DR   AlphaFoldDB; Q7UHE0; -.
DR   STRING; 243090.RB13265; -.
DR   EnsemblBacteria; CAD78033; CAD78033; RB13265.
DR   KEGG; rba:RB13265; -.
DR   PATRIC; fig|243090.15.peg.6427; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_372498_0_0_0; -.
DR   InParanoid; Q7UHE0; -.
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; 3.30.450.20; PAS domain; 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:CAD78033.1};
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   Transferase {ECO:0000313|EMBL:CAD78033.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        87..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        405..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          450..741
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..783
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         479
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   783 AA;  86933 MW;  9B674AE187EE1D00 CRC64;
     MRSVPRRTDA CSMPGDPQRA DTPNSIGKSS IDRHADDRLA NRMSHPQTIG VDGLFPVLDP
     DDVSGGLSNT GLRHSMRPVP WFTRRRVATG ISVLVVLVTA CMAGAILASA IQRATENLVA
     HSLQSVLAAN VHSLEMMFSD LQRESERYSR DERVRQLSLQ LLRGDDQPTP YERESIQHEL
     RAMIPELIGT VPWLIMNRDG LVLGSSRDSI IGLKVEYSKL NHERLIGGKS TLAMPQRISG
     TENETVIMVS MTPLMDRNQC FGAFGWVMEA DDRFSDLLKI TQSGETDESY AIDGRGRMLS
     TSRFEIQLAE KGFPEHSVLN YQMRDPGSDI LANEVIAIPS QELPLTRMAD QAIRRADGME
     LEGYRNYRGA MVVGAWKWLP DFDMAVATEI DVAEAYQPAT ILRRVLIATL AGVVTLSGIA
     LSLIAYSRHR AIRKQRMAEE ESDGRRIGQY RILELLGVGG MGSVYRGQHE YLRRDVAIKV
     LEGERLSTRS VARFHREVQL TSTLRHPNTI AIYDFGQCSA ATGESQVGNS RLGEEVDPEE
     TFYYVMEYID GVSLQQLIDY YGPQTPERTV HFLLQICGSI SEAHSTGLIH RDIKPANILV
     SAHGGLWDHI KVLDFGLVKD IGGDSNLTLQ EGVTRADSMT GTPLYMAPET IRDPAAASPR
     ADIYSIGSVG YALLTGRPIF EGDSVIDLCL KQLEQNPPRP EDRLQQRLPA ALQDILMRCL
     DRSASKRFQT VAECTAALES LPEAGRWTQA KSVEWWANEF DQAARTQPGQ TKNPTVDDAA
     LTR
//