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Database: UniProt
Entry: U2QHW4_9BACT
LinkDB: U2QHW4_9BACT
Original site: U2QHW4_9BACT 
ID   U2QHW4_9BACT            Unreviewed;       853 AA.
AC   U2QHW4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Chain length determinant protein {ECO:0000313|EMBL:ERK38402.1};
GN   ORFNames=HMPREF9135_0857 {ECO:0000313|EMBL:ERK38402.1};
OS   Segatella baroniae F0067.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=1115809 {ECO:0000313|EMBL:ERK38402.1, ECO:0000313|Proteomes:UP000016648};
RN   [1] {ECO:0000313|EMBL:ERK38402.1, ECO:0000313|Proteomes:UP000016648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0067 {ECO:0000313|EMBL:ERK38402.1,
RC   ECO:0000313|Proteomes:UP000016648};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERK38402.1}.
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DR   EMBL; AWEY01000039; ERK38402.1; -; Genomic_DNA.
DR   RefSeq; WP_021590664.1; NZ_AWEY01000039.1.
DR   AlphaFoldDB; U2QHW4; -.
DR   PATRIC; fig|1115809.3.peg.2299; -.
DR   Proteomes; UP000016648; Unassembled WGS sequence.
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   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   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:UP000016648};
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        34..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        514..537
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..113
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          457..534
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          602..756
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
SQ   SEQUENCE   853 AA;  95504 MW;  F57A0D936827CAD2 CRC64;
     MEENKNVVPE KMLEQEERSS FDFQAIYTMV VLNWKWFVLS LMICLGAAYI YLRYATPMYQ
     AYAKLLIKDD DNKRRGNSIE NAVNLGLISN SNGIDNEIEL LASHSLAQAA VRDMKIYTNY
     FVEGNIRSQE LYHTQPFNVD LDAAHLDRLN RPVDMTIEKV GSGYNIVGKY FVPRSEGRAG
     GPYDIDKRVT RIPALVNTRI GVIRITRNML SPMQDLNDRQ VLKVRLMSPK MAAAKYIKNL
     TVNQTSKTTT IAQLTLRDEL PQRATDYLKQ LAIVYNRQAN EDKNEVAQKT EAFINSRLEK
     INAELGSTEG TLENYKRRNN MVELKMNAGQ AVANQDVFAQ KLAEANMQVA LLNEMSLYMN
     QPGNKYEALP SNVGLNDQNA TALINKYNEI AMDRKRLLRS ASETSPTVTP LTAQLDDLGN
     SIRRAMNQSR RNMEIQRNSV AAQFSKYSGD VGATPEQERM LTQIGRQQEV KSGLYLMLLQ
     KREENSISLA ATADKGKLID DPECDGKVSP KSAIIFLIAF VLGLGMPVVV IFVLQFFSYR
     IEGHMDVIRL TKLPIIADIP VASETSKTKA DIVVHENKNN LMEEIFRSLR TNLQFILKGD
     EKVIAFTSTT SGEGKTFTAS NLAVSFALLG RKVILVGLDI RKPRLAELFE IDDHQHGITN
     LLIQANPTEQ DIRKQILASG INHNLELLMA GPTPPNPAEL LTRTSLDSIF EQLRQMYDYV
     IVDTAPVGLV TDTLQIARVT DATVVMTRAD YTAKESVGLV NSLADGNKLP NVCIVINGID
     MSKKKHGYYY GYGKYAKYGR YARLGGSYGN YGRYGGYGAY GSYGRYGSYG SYGSYGNYSN
     SHYGDKNDDS IKK
//
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