ID A0A1I1X7D4_9BACT Unreviewed; 794 AA.
AC A0A1I1X7D4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Capsular exopolysaccharide family {ECO:0000313|EMBL:SFE03272.1};
GN ORFNames=SAMN05518672_104206 {ECO:0000313|EMBL:SFE03272.1};
OS Chitinophaga sp. CF118.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1884367 {ECO:0000313|EMBL:SFE03272.1, ECO:0000313|Proteomes:UP000199596};
RN [1] {ECO:0000313|EMBL:SFE03272.1, ECO:0000313|Proteomes:UP000199596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF118 {ECO:0000313|EMBL:SFE03272.1,
RC ECO:0000313|Proteomes:UP000199596};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FOMK01000004; SFE03272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1X7D4; -.
DR STRING; 1884367.SAMN05518672_104206; -.
DR OrthoDB; 9794577at2; -.
DR Proteomes; UP000199596; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR003856; LPS_length_determ_N_term.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005702; Wzc-like_C.
DR InterPro; IPR033756; YlxH/NBP35.
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 Pfam; PF10609; ParA; 1.
DR Pfam; PF02706; Wzz; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..107
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 429..508
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
SQ SEQUENCE 794 AA; 88392 MW; 28724839061966EC CRC64;
MQRKKTDIRK QQEDQTDLFE LVKNRYLPYW PLFILAAVIA VAGAFVYLRY TTPMYRISAS
LLIKDDQKGM GTSMLESLDL FGSGKQIDNE IEILKSKTLA RQVIRNLNMY GEIIEDGKIK
DVVLYKTIPV KPVFLQPDMI PDLTNTLVPL SYDVATRRLS VNGKSYPLSD TVPTPWGKMV
FLPGNVTEGT HRYFLHVSGE KLLAVQFAGN LKVSQVNKLA NVIGLEYSDV IPARGEAILN
ELMHVYDAAA IDDKNKTATK TMDFVEGRLR IVTSELGQVE SQLARFKTNE GIVDLSEQGK
LFLESVREND SKLNEVNMQL SVLDSIENYV QGRKEGESMV PATLGLTDPV LLELVGKLSE
TEMDLARLKK TTGENSPLLA SLNSQAARLA PAVLENVRNL RSNLRAGREK LQSENNKYMV
VLKGVPMKEK ALLEVGRQQA IKNNIYTFLL EKREETALQY AAAISDSRVV DIAEADSFPF
SPRRSMILGL SFLGGIVLVA GFITLKEMFN SEVMFRADIE KGTATPILAE IMQDQLAHPI
AITEGKRTPV AEQFRALRTG LSYIGINEEH KTILITSSIS GEGKSFIAIN LAISLSLMKK
KVVLLEFDLR KPKVSKMLEV PGQPGISNYL AGQAVLGDIL KLPIENNEYF NLLSCGVIPP
NPTELILNGR LEHLLATLRA TFDYIIIDTA PVGPVTDARL LAPYADATLY VVRHQRTPKF
YLKMIDELYQ QQELGKLNIV FNGIKSRGVS GYSAGYSNGY GYGNGHGYGY GYTDEHKNGN
IRKKRFNKLF NAKS
//