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Database: UniProt
Entry: Q9CM26_PASMU
LinkDB: Q9CM26_PASMU
Original site: Q9CM26_PASMU 
ID   Q9CM26_PASMU            Unreviewed;       699 AA.
AC   Q9CM26;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 117.
DE   SubName: Full=Wzs {ECO:0000313|EMBL:AAK03102.1};
GN   Name=wzs {ECO:0000313|EMBL:AAK03102.1};
GN   OrderedLocusNames=PM1018 {ECO:0000313|EMBL:AAK03102.1};
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843 {ECO:0000313|EMBL:AAK03102.1, ECO:0000313|Proteomes:UP000000809};
RN   [1] {ECO:0000313|EMBL:AAK03102.1, ECO:0000313|Proteomes:UP000000809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70 {ECO:0000313|EMBL:AAK03102.1,
RC   ECO:0000313|Proteomes:UP000000809};
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
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DR   EMBL; AE004439; AAK03102.1; -; Genomic_DNA.
DR   RefSeq; WP_010906974.1; NC_002663.1.
DR   AlphaFoldDB; Q9CM26; -.
DR   STRING; 272843.PM1018; -.
DR   EnsemblBacteria; AAK03102; AAK03102; PM1018.
DR   KEGG; pmu:PM1018; -.
DR   PATRIC; fig|272843.6.peg.1031; -.
DR   HOGENOM; CLU_009912_0_0_6; -.
DR   OMA; QQIYIQL; -.
DR   OrthoDB; 9775724at2; -.
DR   Proteomes; UP000000809; Chromosome.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05387; BY-kinase; 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   Reference proteome {ECO:0000313|Proteomes:UP000000809};
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        24..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..97
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          360..440
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          526..636
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   COILED          248..282
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          334..364
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   699 AA;  78079 MW;  BA8A9E5E934199E1 CRC64;
     MNEKNHEETL DVMKFLGILL DHKGWIALFT LLTTLIGAGY AFLAPPVYLA NASIQIEDKS
     AGGALKDFAG IFEEKSSSHT EIAILKSRMV LSYAVEKLDL TTQVEPIYPI PILGKLFASA
     TGYSPQITIS HFTPLNEAAN TLILEIGEQR DSYTLFLEKT TEPLLTGKVG EKYDTDLIQF
     SLSQINAKPK QRFLINKLPE LTVISALQEQ LSVHEIGKQT GIINIAIQGK DKKHIQDIVS
     SIAESYLLQN VARNSAEASK SLEFLNQQLP DVRQKLSDSE NRLNEFRLKN ESVDLSLEAK
     ATLDTIIQIE ADLSELSIQE SEISRKFTLK HPSYVALIDK RNVLNAEKER LNKQLEKLPN
     TQKEMIRFTR DLEVNQHIYI QLLNKMQELD VVKASTIGNV RILDHAQVFP NPVAPKKALV
     IILAFLLGGL LSSFLVLFRN YFQRGIESTA DVDKTGLPTY AAIPYSEQQP AVSRKHVHKG
     KYRLLSESHP EDNAIEAIRS LRTSLHFAML EAPNNLVMIS GTLPSVGKSF ISSNLANVLA
     KTGKRVLLID ADLRRSYLRP FLGIANKQGL SEAIAQNIPF EDIVHQYAEF AIITKGNTPP
     NPSELFYTAR FQQLLEWASS HYDLVVIDTP PILPVTDAAI IGRYVGTTLL VGLFGKTTVK
     EIEIAKTRFA QAGVPVKGFI LNGTKRKALS YYDYYNYRS
//
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