ID A0A101ID04_9BACT Unreviewed; 737 AA.
AC A0A101ID04;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Capsular exopolysaccharide biosynthesis protein {ECO:0000313|EMBL:KUK92946.1};
GN ORFNames=XE05_1231 {ECO:0000313|EMBL:KUK92946.1};
OS Thermotogales bacterium 46_20.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales.
OX NCBI_TaxID=1635293 {ECO:0000313|EMBL:KUK92946.1, ECO:0000313|Proteomes:UP000054930};
RN [1] {ECO:0000313|Proteomes:UP000054930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK92946.1}.
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; LGGZ01000078; KUK92946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101ID04; -.
DR Proteomes; UP000054930; 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 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 25..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..101
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 393..470
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 535..656
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 289..337
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 737 AA; 82168 MW; 52ECCC8C38D1FD4A CRC64;
MNQTNGDDYR ELTLEDILRI FRKRLLLFFL VVVGVVVATG IYLFLATPIY EASVTIKVDP
ATRSSIDIFT AGLTGTTSSR DIATEIELIK SRSNFETVIE RLELVERIYT SFEIQEMLSE
GYTQNDIEAS LAKTLSNITS VSPVKDTRIV RVSVQHRDRT IARDVANTLA EVYNEKLAEL
SRRDATTRRE FIESQIPSVE EQVRRSSDAL REFKEKTGIY VLDAQARWLL DMLSNYDKQF
NALVIELEEK KAEVVAYQKL LDEFDSPEAG ALQEKWINTS HTLSLNPVIT QLRNKLALLK
VDLAALEDQY PATDQRIRAK KAEIAATEKL IQEEIENEFI RTGEGMSLNP TYQTILTAVI
TSETSLQIIE STIQSVDMLR KTYLDALAEI PRLEQQLLEL QREVYISENL YTLLLERLEE
AKISEAAVIG NAAVIDSALI PSAPVKPNRR LSLAIGGVLG IFLGMLGVFL AEYLDKTLKS
EEDIERVASE PILGRIPLAN GIRNELFVQS DPTSPPSEAV KIASSNISFT LGDGKVIGVT
SPLPGEGKTT VAANIAYSYA MSGQRVLLVD LDMRKPRIEQ LLGMDDRSSE GIVDIVLDNR
NVGDLIIKYA ENLDVLPVGK IPPNPTVLLS SKKIAALIEG LKNEYDRIIV DLPPAVITSD
VALVGHLFDG VLMVTQPGTT LRDALRMAIS NLKTSGAKVL GFVVNGVTVK TSGYYYHYYY
YHYSEGTKKR KEHRKVR
//
