ID R5GSU5_9BACT Unreviewed; 824 AA.
AC R5GSU5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative tyrosine-protein kinase ptk {ECO:0000313|EMBL:CCY15842.1};
GN ORFNames=BN773_00103 {ECO:0000313|EMBL:CCY15842.1};
OS Prevotella sp. CAG:755.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262935 {ECO:0000313|EMBL:CCY15842.1, ECO:0000313|Proteomes:UP000018353};
RN [1] {ECO:0000313|EMBL:CCY15842.1, ECO:0000313|Proteomes:UP000018353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:755 {ECO:0000313|Proteomes:UP000018353};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCY15842.1}.
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DR EMBL; CAXR010000101; CCY15842.1; -; Genomic_DNA.
DR AlphaFoldDB; R5GSU5; -.
DR STRING; 1262935.BN773_00103; -.
DR Proteomes; UP000018353; 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, ECO:0000313|EMBL:CCY15842.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018353};
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 36..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 509..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..119
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 458..530
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 603..728
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 824 AA; 92988 MW; 8069FCB162B3B672 CRC64;
MANQNYINPP AVQQETEDID WLSIVRACTG TLRRQWRWFV FSIIVCGCLA FLYERKQPRV
YQRQAVIEIE GADGSSGSRR MPSNMNALLE LNGITAGDQL QNEIFILQSH RLIERVVTRL
KLDVDYSVKN GLGQSTLYKK RPFEATFLRP AEIDEDITFK VDLIDNQKFR IFDVRYKDED
CRIDKVVAYG QRIATPAGNV YLTRKMNLEG LEPTTVTVSR LPVFTATEMY RSKLSCGEID
KESSLIVLTF QDTNKKRAED FLNVLLDVYK EDIIDGKNRI AESTAIFIDS RIKIIGDELN
DVEGSLARFK ERNQIVDFEK SAQSALEEQR TLRLSMLQAE VQLSVAEYLE DFLKNNSKAD
QVIPVLNDMV DQGIQQQITE YNKLVLERNR LAPNTGENSP VMNDLNQKLI ATNEAIRASV
HSLVNTLRLR AESARRNENT FNTILSGVPN IEKSAGDIKR QQEIKSALYS YLLNKREEVA
LQLAINEANI RTVEYPLGFE RPVAPHSMII MAIGLFIGIL IPTAVFTIRS YMDTAVRGRK
DIEDATDLNV IGEIPRWEDA NKLGDSETLI ATDETNNTVT EAFRMLRYGL SFIRKHNQVV
MCTSATPGQG KTFVSRNLAA ILARADKRVI LIDADIRKRT QSKQLGNRFG LTSYLNGDIT
RVEEIIISRG GTNLQDVDFI PAGLLPPNPA ELLMDARFDE LIDELRSRYD YIIIDTTPAL
QVADAGIVSR VADQTLFIIR VGVQDRHFLP TLQRLSDDKQ LGNISVVLND CVNNVLGYGY
GYGYGYGYGH TAGRQNHAKH GNKSSGLSKK LSAGVLHRLN NRKQ
//
