YC06_KLEPN
ID YC06_KLEPN Reviewed; 722 AA.
AC Q48452;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Putative tyrosine-protein kinase in cps region;
DE EC=2.7.10.-;
DE AltName: Full=ORF6;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Chedid;
RX PubMed=7896702; DOI=10.1128/jb.177.7.1788-1796.1995;
RA Arakawa Y., Wacharotayankun R., Nagatsuka T., Ito H., Kato N., Ohta M.;
RT "Genomic organization of the Klebsiella pneumoniae cps region responsible
RT for serotype K2 capsular polysaccharide synthesis in the virulent strain
RT Chedid.";
RL J. Bacteriol. 177:1788-1796(1995).
RN [2]
RP PHOSPHORYLATION.
RX PubMed=11742763; DOI=10.1016/s1096-4959(01)00490-0;
RA Preneta R., Jarraud S., Vincent C., Doublet P., Duclos B., Etienne J.,
RA Cozzone A.J.;
RT "Isolation and characterization of a protein-tyrosine kinase and a
RT phosphotyrosine-protein phosphatase from Klebsiella pneumoniae.";
RL Comp. Biochem. Physiol. 131B:103-112(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC -!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated on tyrosine residue(s).
CC {ECO:0000269|PubMed:11742763}.
CC -!- SIMILARITY: Belongs to the etk/wzc family. {ECO:0000305}.
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DR EMBL; D21242; BAA04777.1; -; Genomic_DNA.
DR AlphaFoldDB; Q48452; -.
DR SMR; Q48452; -.
DR UniPathway; UPA00631; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR025669; AAA_dom.
DR InterPro; IPR005702; EPS_synthesis.
DR InterPro; IPR032807; GNVR.
DR InterPro; IPR003856; LPS_length_determ_N_term.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13614; AAA_31; 1.
DR Pfam; PF13807; GNVR; 1.
DR Pfam; PF02706; Wzz; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01007; eps_fam; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane;
KW Exopolysaccharide synthesis; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT CHAIN 1..722
FT /note="Putative tyrosine-protein kinase in cps region"
FT /id="PRO_0000212360"
FT TRANSMEM 31..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..449
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 722 AA; 80400 MW; 3CAD6910AE81C3D7 CRC64;
MTSISKKKQP ETVDDLDFGR MVGELIDHRK IIIALTSFAT LIALLYAFFA TPIYKADALI
QVEQKQANAI LSNLSQMLPD SQPQSAPEIA LIQSRMILGK TVDDLNLQAV VSPKYFPIFG
RGWARLSGEH QGNIQLSRLY VSSSIGDEEN PPEFTLKVKD SNRYVIEFGG EEINGKVGEL
IEKDGITLKI DEINAKPGAE FTIKYVSKLK AIADLQENLS VADQGKDTGI LILSYLGDDP
LKIKNIVDSI SENYLAQNIS RQAAQDEKSL EFLNKQLPMV RSDLDSAEDK LNDFRKRNDS
VDLSLEAKSV LDQIVNVDNQ LNELTFRESE ISQLYTKEHP TYKALMEKRK TLQDERGKLN
KRVATMPETQ QEILRLSRDV ESGRAVYMQL LNRQQELNIA KSSAIGNVRI IDSAVTQHKP
VKPKKIIVVL AGLFIGLVIS VSLVLVRILL RKGIETPEQL EELGINVYAS IPVSESNPKN
VIAKRLNKRD DSRPKVLLAT ENPADLAIEA IRGLRTSLHF AMLEARNNLL MISGASPNAG
KTFVSSNLSS VISQTGKKVI FIDADLRKGY THKLFNIKNT NGLSDYLSGR VALDKIINNL
QTEGFDYISR GSVPPNPAEL LMHNRLAELL EWANKSYDIV ILDTPPILAV ADAAIIGNYV
GTTLLVARFE ENTPKEIDIS VKRFQNSGVN IKGCILNGVV KKATNKYGYG YNYYDYSYSD
KK