PRKC_BACAN
ID PRKC_BACAN Reviewed; 657 AA.
AC Q81WH6; Q6HUM4; Q6KNV8;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
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=BA_4000, GBAA_4000, BAS3713;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [4]
RP FUNCTION IN PEPTIDOGLYCAN-DEPENDENT GERMINATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Sterne;
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: Protein kinase that is responsible for triggering spore
CC germination in response to muropeptides, signaling bacteria to exit
CC dormancy. PrkC is thus a germination receptor that binds peptidoglycan
CC fragments containing m-Dpm (meso-diaminopimelate), which act as spore
CC germinants. Probably autophosphorylates and phosphorylates FusA (EF-G,
CC elongation factor G); the latter modification is likely necessary for
CC germination in response to peptidoglycan.
CC {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. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Spores lacking this gene fail to germinate in the
CC presence of peptidoglycan fragments. {ECO:0000269|PubMed:18984160}.
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; AE016879; AAP27728.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33115.2; -; Genomic_DNA.
DR EMBL; AE017225; AAT56015.1; -; Genomic_DNA.
DR RefSeq; NP_846242.1; NC_003997.3.
DR RefSeq; WP_000904759.1; NZ_QPKQ01000003.1.
DR RefSeq; YP_029964.1; NC_005945.1.
DR AlphaFoldDB; Q81WH6; -.
DR SMR; Q81WH6; -.
DR IntAct; Q81WH6; 1.
DR STRING; 260799.BAS3713; -.
DR EnsemblBacteria; AAP27728; AAP27728; BA_4000.
DR EnsemblBacteria; AAT33115; AAT33115; GBAA_4000.
DR GeneID; 45023691; -.
DR KEGG; ban:BA_4000; -.
DR KEGG; bar:GBAA_4000; -.
DR KEGG; bat:BAS3713; -.
DR PATRIC; fig|198094.11.peg.3970; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR OMA; DPDYRYQ; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; ISS: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; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR GO; GO:0009847; P:spore germination; IMP:UniProtKB.
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 Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..657
FT /note="Serine/threonine-protein kinase PrkC"
FT /id="PRO_0000398661"
FT TOPO_DOM 1..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..657
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 11..282
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 365..432
FT /note="PASTA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 433..499
FT /note="PASTA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 500..566
FT /note="PASTA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 40
FT /note="Required for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 162
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 163
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 165
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 167
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 214
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 290
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 657 AA; 74153 MW; 20788151AFAF5503 CRC64;
MLIGKRLNDR YKLLKMIGGG GMANVYLAHD DILGRDVAVK ILRLDYSNNE EFIKRFHREA
QSVTTLSHPN IVNMYDVGEE DGIYYLVMEY VPGQTLKQYI IERGMLPIGE ALDIMEQLTS
AMAHAHHFEI VHRDIKPHNI LIRADGVIKV TDFGIATATS ATTITHTNSV LGSVHYLSPE
QARGGIANKQ SDIYSLGIVM FELLTGRQPF SGESAVAIAL KHLQSEIPSP KRWNENIPQS
VENIILKATA KDPFHRYQSA NAMKRDIETA LYPERINEQP FYIPEDMEAT KAIPIIQQEQ
LFENVTDETI VLKGSKVDEQ IRKEETDLSK KKKRSNKWLK ILITTFLLLA IGITLALTVI
PGFFIPKDVK VPDVAGMKYT TAVNTLVEKG FEVTEPNIVY TDDVETGDVI KTDPVAGRVV
KENSKITIYQ SGGKKKSKMI DFTGKDLESI RTELEEKYKQ VTVYYIEDDR PKGAIVEQIP
TSDQMVVEAE QELKIWVSKG PYQIRPGDFS RWTENSVTGY LNERKLTPDI KREYSDTVDK
GLVISQSPKP GTPLKEGDKV TIIISEGPKP KVTKTVKVDN ISIPYESSII GEKKPQTIEI
YKEDMQQKMD RPIETRTISE SATISLEFVI QEDTKGRYKI VRDGVTIIDK EVPYPTQ
