ID F4C8A0_SPHS2 Unreviewed; 789 AA.
AC F4C8A0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Capsular exopolysaccharide family {ECO:0000313|EMBL:ADZ78372.1};
DE EC=2.7.10.2 {ECO:0000313|EMBL:ADZ78372.1};
GN OrderedLocusNames=Sph21_1810 {ECO:0000313|EMBL:ADZ78372.1};
OS Sphingobacterium sp. (strain 21).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ78372.1};
RN [1] {ECO:0000313|EMBL:ADZ78372.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=21 {ECO:0000313|EMBL:ADZ78372.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT "Complete sequence of Sphingobacterium sp. 21.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002584; ADZ78372.1; -; Genomic_DNA.
DR AlphaFoldDB; F4C8A0; -.
DR STRING; 743722.Sph21_1810; -.
DR KEGG; shg:Sph21_1810; -.
DR PATRIC; fig|743722.3.peg.1936; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_6_0_10; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd05387; BY-kinase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR032807; GNVR.
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; PF13807; GNVR; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000313|EMBL:ADZ78372.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 432..511
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT COILED 273..323
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 383..418
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 789 AA; 89664 MW; 3C8BBCC3A1FFE055 CRC64;
MNDNFSSSHH EKTELNIKAI LLNYLRHWQW FAISLFGCIL FAFIYFKYTT PQYEIRSTLL
IKDDKKAPGM GGANVFEDLD IFRSNQNVNN EIEVLRGKTL MQRALTELHL DISYFDKESL
RKTELYGKSL PVKVLVSKLD SSAYLLEDGI SIYTIDDNSF ELDDSVKNRY SFGQPIKRGY
ATFTVLKGPA FEKDRSVLFR FVNLRQLALS YSSRLNIETV NKDGSVISLS LIEPVIDKGR
DVINRLVQVY NKEAVEDKNQ LADKTVKFID ERLSYLVGEL SNVEKNVEKY KKEHEITNVS
AEAEQYLKEA GDYSRKLAEA STQLNILESI QNYLSEQENK NELVPSALGI QDPTLNGLIA
KFNEMQLERQ RLMRTTQEGN PLVESLDEQL ANLRENILEN LQNIKSGFQI TLQSLKENSG
QFRSRIQNVP SIERNLLEIQ REQGIKEALY TYLLQKREES AISLASAVSN TRIIDPAMAG
DQPVKPRKII ILFFSFIMGI AIPIGVLYIK DLLNDKVTLM SDVQEAVPVP ILGELIHNED
EQHTLVVNKS SRTPLAELFR LIRTNLQFAT LGKENKVILI TSSMTREGKT FFSINMGASM
ALTGKRVVLL EFDIRKPKLI KDLGIPVPKK GITNYLVDKA ITVGDLVNDT KLVDNLFVIG
AGPIPPNPAE LLLSSRIDEL FNTLKENFDC IIVDTSPVGQ VADAFTLAKQ ADMGIYMVRY
NYTFKQQLNI VKDVYENKKI PNLNIVLNDA KEENAYGYGY GYGYGYGYGA ELDEKRNWLS
RIKKYLKRG
//
