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Serine/threonine-protein kinase PknB (EC 2.7.11.1)

 PKNB_MYCS2              Reviewed;         625 AA.
A0QNG1;
24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 1.
20-JUN-2018, entry version 85.
RecName: Full=Serine/threonine-protein kinase PknB;
EC=2.7.11.1;
Name=pknB; OrderedLocusNames=MSMEG_0028, MSMEI_0031;
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycolicibacterium.
NCBI_TaxID=246196;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700084 / mc(2)155;
Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
Fraser C.M.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700084 / mc(2)155;
PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
"Interrupted coding sequences in Mycobacterium smegmatis: authentic
mutations or sequencing errors?";
Genome Biol. 8:R20.1-R20.9(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700084 / mc(2)155;
PubMed=18955433; DOI=10.1101/gr.081901.108;
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
"Ortho-proteogenomics: multiple proteomes investigation through
orthology and a new MS-based protocol.";
Genome Res. 19:128-135(2009).
[4]
PROBABLE FUNCTION AS A KINASE WITH RSEA AS A SUBSTRATE, ENZYME
REGULATION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 700084 / mc(2)155;
PubMed=20025669; DOI=10.1111/j.1365-2958.2009.07008.x;
Barik S., Sureka K., Mukherjee P., Basu J., Kundu M.;
"RseA, the SigE specific anti-sigma factor of Mycobacterium
tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2
proteolysis.";
Mol. Microbiol. 75:592-606(2010).
-!- FUNCTION: Protein kinase that regulates many aspects of
mycobacterial physiology. Is a key component of a signal
transduction pathway that regulates cell growth, cell shape and
cell division via phosphorylation of target proteins (By
similarity). Probably phosphorylates RseA (PubMed:20025669).
{ECO:0000250|UniProtKB:P9WI81, ECO:0000305|PubMed:20025669}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: By K-252a. {ECO:0000305|PubMed:20025669}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
membrane protein {ECO:0000305}.
-!- DOMAIN: The PASTA domains interact with peptidoglycans and are
required for PknB localization. {ECO:0000250}.
-!- PTM: Autophosphorylated. Dephosphorylated by PstP (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: When depleted (with anti-sense RNA) no
vancomycin-induced degradation of RseA is seen.
{ECO:0000269|PubMed:20025669}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; CP000480; ABK74027.1; -; Genomic_DNA.
EMBL; CP001663; AFP36514.1; -; Genomic_DNA.
RefSeq; WP_003891355.1; NZ_CP009494.1.
RefSeq; YP_884449.1; NC_008596.1.
ProteinModelPortal; A0QNG1; -.
SMR; A0QNG1; -.
STRING; 246196.MSMEG_0028; -.
EnsemblBacteria; ABK74027; ABK74027; MSMEG_0028.
EnsemblBacteria; AFP36514; AFP36514; MSMEI_0031.
GeneID; 4536298; -.
KEGG; msb:LJ00_00145; -.
KEGG; msg:MSMEI_0031; -.
KEGG; msm:MSMEG_0028; -.
PATRIC; fig|246196.19.peg.27; -.
eggNOG; ENOG4105D9P; Bacteria.
eggNOG; COG0515; LUCA.
eggNOG; COG2815; LUCA.
HOGENOM; HOG000037185; -.
KO; K12132; -.
OMA; ICAKAMA; -.
OrthoDB; POG091H0264; -.
Proteomes; UP000000757; Chromosome.
Proteomes; UP000006158; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR005543; PASTA_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF03793; PASTA; 4.
Pfam; PF00069; Pkinase; 1.
SMART; SM00740; PASTA; 4.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51178; PASTA; 4.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Kinase; Magnesium;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 625 Serine/threonine-protein kinase PknB.
/FTId=PRO_0000422953.
TOPO_DOM 1 331 Cytoplasmic. {ECO:0000255}.
TRANSMEM 332 352 Helical. {ECO:0000255}.
TOPO_DOM 353 625 Extracellular. {ECO:0000255}.
DOMAIN 11 274 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 355 421 PASTA 1. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
DOMAIN 422 489 PASTA 2. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
DOMAIN 490 556 PASTA 3. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
DOMAIN 557 625 PASTA 4. {ECO:0000255|PROSITE-
ProRule:PRU00528}.
NP_BIND 17 25 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 93 95 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 140 143 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 138 138 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
METAL 143 143 Magnesium. {ECO:0000250}.
METAL 156 156 Magnesium. {ECO:0000250}.
BINDING 40 40 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 156 156 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 169 169 Phosphoserine; by autocatalysis.
{ECO:0000250}.
MOD_RES 171 171 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
MOD_RES 173 173 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
MOD_RES 294 294 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
MOD_RES 295 295 Phosphoserine; by autocatalysis.
{ECO:0000250}.
MOD_RES 309 309 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
SEQUENCE 625 AA; 66318 MW; E9B75950ADF718DA CRC64;
MTTPQHLSDR YELGEILGFG GMSEVHLARD LRLHRDVAVK VLRADLARDP SFYLRFRREA
QNAAALNHPA IVAVYDTGEA ETPNGPLPYI VMEYVDGVTL RDIVHTDGPI APRRAIEIIA
DACQALNFSH QHGIIHRDVK PANIMISKNN AVKVMDFGIA RALADTGNSV TQTAAVIGTA
QYLSPEQARG ETVDARSDVY SLGCVLYEIL TGEPPFIGDS PVAVAYQHVR EDPVPPSRRH
ADVTPELDAV VLKALAKNPD NRYQTAAEMR ADLIRVHEGQ APDAPKVLTD AERTSMLAAP
PADRAGAATQ DMPVPRPAGY SKQRSTSVAR WLIAVAVLAV LTVVVTVAIN MVGGNPRNVQ
VPDVAEQSAD DAQAALQNRG FKTVIDRQPD NEVPPGLVIG TDPEAGSELG AGEQVTINVS
TGPEQALVPD VAGLTPTQAR QKLKDAGFEK FRESPSPSTP EQKGRVLATN PQANQTAAII
NEITIVVGAG PEDAPVLSCA GQNAESCKAI LAAGGFTNTV VVEVDNPAAA GQVVGTEPAD
GQSVPKDTVI QIRVSKGNQF VMPDLVGQFW SDAYPRLTAL GWTGVLDKGP DVRDSGQRTN
AVVTQSPSAG TPVNKDAKIT LSFAA


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