ID A2V7T4_KLEPN Unreviewed; 723 AA.
AC A2V7T4;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Putative transmembrane protein {ECO:0000313|EMBL:BAF47014.1};
GN Name=wzc {ECO:0000313|EMBL:BAF47014.1};
OS Klebsiella pneumoniae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573 {ECO:0000313|EMBL:BAF47014.1};
RN [1] {ECO:0000313|EMBL:BAF47014.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=889/50 {ECO:0000313|EMBL:BAF47014.1};
RX PubMed=17599305; DOI=10.1086/519262;
RA Fang C.T., Lai S.Y., Yi W.C., Hsueh P.R., Liu K.L., Chang S.C.;
RT "Klebsiella pneumoniae genotype K1: an emerging pathogen that causes septic
RT ocular or central nervous system complications from pyogenic liver
RT abscess.";
RL Clin. Infect. Dis. 45:284-293(2007).
RN [2] {ECO:0000313|EMBL:BAF47014.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=889/50 {ECO:0000313|EMBL:BAF47014.1};
RA Fang C.T., Lai S.Y., Yi W.C.;
RT "Complete nucleotide sequences of Klebsiella pneumoniae serotype K20
RT capsular polysaccharides biosynthesis gene cluster, Statens Serum Institut
RT (Denmark) serotype K20 reference strain.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001074};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the etk/wzc family.
CC {ECO:0000256|ARBA:ARBA00008883}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB289647; BAF47014.1; -; Genomic_DNA.
DR AlphaFoldDB; A2V7T4; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05387; BY-kinase; 1.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR025669; AAA_dom.
DR InterPro; IPR032807; GNVR.
DR InterPro; IPR003856; LPS_length_determ_N_term.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005702; Wzc-like_C.
DR NCBIfam; TIGR01007; eps_fam; 1.
DR PANTHER; PTHR32309; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR32309:SF13; TYROSINE-PROTEIN KINASE ETK-RELATED; 1.
DR Pfam; PF13614; AAA_31; 1.
DR Pfam; PF13807; GNVR; 1.
DR Pfam; PF02706; Wzz; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 32..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..106
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 370..449
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 538..652
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 271..305
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 723 AA; 79756 MW; 6BDB319247DD4621 CRC64;
MTSVTSKKST ILGSDEIDLG RVIGELIDHR KLIISITSVF TLFAILYALL ATPIYETDAL
IQIEQKQGNA ILSSLSQVLP DGQPQSAPET ALLQSRMILG KTIDDLNLQI QIKQKYFPVI
GRGLARLMGE KPGNIDITRL YLPGSDDISN NTPSIILTVK DKENYSINSD GIQLNGVVGT
LLNEKGISLL VNEIDAKPGD QFVITQLPRL KAISDLLKSF SVADLGKDTG MLTLTLTGDN
PKRISHILDS ISQNYLAQNI ARQAAQDAKS LEFLNQQLPK VRAELDSAED KLNAYRKQKD
SVDLNMEAKS VLDQIVNVDN QLNELTFREA EVSQLYTKEH PTYKALMEKR QTLQEEKSKL
NKRVSSMPST QQEVLRLSRD VESGRAVYLQ LLNRQQELNI AKSSAIGNVR IIDNAVTDPN
PVRPKKTIII VIGVVLGLIV SVVLVLFQVF LRRGIESPEQ LEEIGINVYA SIPISEWLAK
NARQSGKVRK NQSDTLLAVG NPADLAVEAI RGLRTSLHFA MMEAKNNVLM ISGASQSAGK
TFISNNLAAT IAITGKKVLF IDADLRKGYA HKMFGHKNDK GLSEFLSGQA AAEMVIDKVE
GGEFDYIGRG QIPPNPAELL MHPRFEQLLN WASQNYDLII IDTPPILAVT DAAIIGRYAG
TCLLVARFEK NTVKEIDVSM KRFEQSGVVV KGCILNGVVK KASSYYGYGY NHYGYSYSDK
KID
//
