ID PRKC_STAAE Reviewed; 664 AA.
AC A6QGC0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Serine/threonine-protein kinase PrkC;
DE Short=Ser/Thr-protein kinase PrkC;
DE EC=2.7.11.1;
GN Name=prkC; OrderedLocusNames=NWMN_1130;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [2]
RP FUNCTION IN PEPTIDOGLYCAN-DEPENDENT GERMINATION, AND PEPTIDOGLYCAN-BINDING.
RX PubMed=18984160; DOI=10.1016/j.cell.2008.08.039;
RA Shah I.M., Laaberki M.H., Popham D.L., Dworkin J.;
RT "A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in
RT response to peptidoglycan fragments.";
RL Cell 135:486-496(2008).
CC -!- FUNCTION: Probable protein kinase that is responsible for triggering
CC spore germination in response to muropeptides, signaling bacteria to
CC exit dormancy. PrkC is thus a germination receptor that binds
CC peptidoglycan fragments containing either m-Dpm (meso-diaminopimelate)
CC or L-lys, which act as spore germinants. Probably autophosphorylates
CC and phosphorylates FusA (EF-G, elongation factor G); the latter
CC modification is likely necessary for germination in response to
CC peptidoglycan. {ECO:0000269|PubMed:18984160}.
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 -!- 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;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Spore membrane; Single-pass type II membrane
CC protein. Note=Is associated with the inner membrane of the spore.
CC {ECO:0000250}.
CC -!- DOMAIN: The C-terminal extracellular domain containing the PASTA
CC repeats binds peptidoglycan.
CC -!- MISCELLANEOUS: PubMed:18984160 shows that peptidoglycan fragments serve
CC as a novel mechanism of interspecies bacterial signaling that likely
CC indicates the presence of growing bacteria and thus serve as a signal
CC for dormant cells that growth-promoting conditions exist.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AP009351; BAF67402.1; -; Genomic_DNA.
DR RefSeq; WP_000579564.1; NZ_CP023390.1.
DR AlphaFoldDB; A6QGC0; -.
DR SMR; A6QGC0; -.
DR KEGG; sae:NWMN_1130; -.
DR HOGENOM; CLU_000288_135_2_9; -.
DR Proteomes; UP000006386; Chromosome.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0071224; P:cellular response to peptidoglycan; IGI:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IGI:UniProtKB.
DR GO; GO:0009847; P:spore germination; IGI:UniProtKB.
DR CDD; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.60.40.2560; -; 1.
DR Gene3D; 3.30.10.20; -; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR045269; Atg1-like.
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; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF21160; PrkC-like_PASTA-like; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 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 1: Evidence at protein level;
KW ATP-binding; Germination; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Repeat; Serine/threonine-protein kinase; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..664
FT /note="Serine/threonine-protein kinase PrkC"
FT /id="PRO_0000398662"
FT TOPO_DOM 1..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..664
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 10..271
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 373..440
FT /note="PASTA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 441..509
FT /note="PASTA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 510..575
FT /note="PASTA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT REGION 541..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 16..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 39
FT /note="Required for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 161
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 164
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 166
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 664 AA; 74363 MW; 26F1386C5DB61828 CRC64;
MIGKIINERY KIVDKLGGGG MSTVYLAEDT ILNIKVAIKA IFIPPREKEE TLKRFEREVH
NSSQLSHQNI VSMIDVDEED DCYYLVMEYI EGPTLSEYIE SHGPLSVDTA INFTNQILDG
IKHAHDMRIV HRDIKPQNIL IDSNKTLKIF DFGIAKALSE TSLTQTNHVL GTVQYFSPEQ
AKGEATDECT DIYSIGIVLY EMLVGEPPFN GETAVSIAIK HIQDSVPNVT TDVRKDIPQS
LSNVILRATE KDKANRYKTI QEMKDDLSSV LHENRANEDV YELDKMKTIA VPLKKEDLAK
HISEHKSNQP KRETTQVPIV NGPAHHQQFQ KPEGTVYEPK PKKKSTRKIV LLSLIFSLLM
IALVSFVAMA MFGNKYEETP DVIGKSVKEA EQIFNKNNLK LGKISRSYSD KYPENEIIKT
TPNTGERVER GDSVDVVISK GPEKVKMPNV IGLPKEEALQ KLKSLGLKDV TIEKVYNNQA
PKGYIANQSV TANTEIAIHD SNIKLYESLG IKQVYVEDFE HKSFSKAKKA LEEKGFKVES
KEEYSDDIDE GDVISQSPKG KSVDEGSTIS FVVSKGKKSD SSDVKTTTES VDVPYTGKND
KSQKVKVYIK DKDNDGSTEK GSFDITSDQR IDIPLRIEKG KTASYIVKVD GKTVAEKEVS
YDDV
//
