ID E6UA92_RUMA7 Unreviewed; 736 AA.
AC E6UA92;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=Rumal_1816 {ECO:0000313|EMBL:ADU22314.1};
OS Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 /
OS 7).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=697329 {ECO:0000313|EMBL:ADU22314.1, ECO:0000313|Proteomes:UP000006919};
RN [1] {ECO:0000313|EMBL:ADU22314.1, ECO:0000313|Proteomes:UP000006919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7
RC {ECO:0000313|Proteomes:UP000006919};
RX PubMed=21914885; DOI=10.1128/JB.05621-11;
RA Suen G., Stevenson D.M., Bruce D.C., Chertkov O., Copeland A., Cheng J.F.,
RA Detter C., Detter J.C., Goodwin L.A., Han C.S., Hauser L.J., Ivanova N.N.,
RA Kyrpides N.C., Land M.L., Lapidus A., Lucas S., Ovchinnikova G.,
RA Pitluck S., Tapia R., Woyke T., Boyum J., Mead D., Weimer P.J.;
RT "Complete genome of the cellulolytic ruminal bacterium Ruminococcus albus
RT 7.";
RL J. Bacteriol. 193:5574-5575(2011).
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; CP002403; ADU22314.1; -; Genomic_DNA.
DR RefSeq; WP_013498478.1; NZ_JHYT01000009.1.
DR AlphaFoldDB; E6UA92; -.
DR STRING; 697329.Rumal_1816; -.
DR KEGG; ral:Rumal_1816; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000006919; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 3.
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:ADU22314.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ADU22314.1};
KW Transferase {ECO:0000313|EMBL:ADU22314.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 343..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..273
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 382..447
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 448..514
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 518..582
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 302..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..334
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 736 AA; 81329 MW; 70201C9D9C75F0B2 CRC64;
MDSNIGKKLD GRYEITELIG VGGMADVYKA QDIMEDRPVA VKILKPEFSG DEEFLRRFRN
ESKAIAVLSH PNIVKIYDVG FTDEIQFIVM EYIDGITLKE FIEQQGVLKW KDALHFITQI
LRALQHAHDK GIVHRDIKPQ NIMLFTDGTI KVMDFGIARF SRIDGKTLSD KAIGSVHYIS
PEQAQGEMTD ERSDIYSVGV MLYEMLTGRK PFDGDTAVNV ALKHMQEVAV PPREIMPSIP
EALEEIVYHA MEKQPAQRYQ SAAEMIRDID TFKLNQSVVF GYKDGSAPVV DNVGFYPVNN
NQSRKPVIND DYDDYDDDYE DDYDDDDYDD DDDDDESGKK RSYVVPILLA VTVAVVIVAA
FIIGWTVIKA FSPKDGSGFG IHTSTITVPN LVGENIIKVE GDFKDKLKIE TIEEYNFEYE
KDTIFWQSIS PQKSVKEGTT ITLKVSKGKQ MIVIPDVSGS ETEIAESELR AAGFTVVLRS
KYDDKVPDGI AIGTEPVAGT EFASDGAVTL YVSKGPLDTQ VKVPNVVGLT KEKAIAILKD
SKLKANVQDM PHDGDKGKVI DQSIEADRRV ERDSEITIYV STGETDPVDL TISLPMPEGM
HGSYSIEVFV NGNVRYNQKI NNGESVAGGN VTIDISGKKT ETLTVSIRND ETGKSVNYAV
FNVNYDKKTA ELNGSLNKDG LIAITPSVKE EPSKPDESSS QADPVPPQPV DPEPPVSDDS
SQADVPPVDN GGENIF
//
