ID A0A0A3W290_9GAMM Unreviewed; 607 AA.
AC A0A0A3W290;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Polysaccharide biosynthesis protein CapD-like domain-containing protein {ECO:0000259|Pfam:PF02719};
GN ORFNames=GW12_14190 {ECO:0000313|EMBL:KGT47507.1};
OS Acinetobacter sp. HR7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1509403 {ECO:0000313|EMBL:KGT47507.1, ECO:0000313|Proteomes:UP000032870};
RN [1] {ECO:0000313|EMBL:KGT47507.1, ECO:0000313|Proteomes:UP000032870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR7 {ECO:0000313|EMBL:KGT47507.1,
RC ECO:0000313|Proteomes:UP000032870};
RA Ahn S., Kim B.-C.;
RT "Genome sequencing of Acinetobacter sp. strain HR7.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC {ECO:0000256|ARBA:ARBA00007430}.
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:KGT47507.1}.
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DR EMBL; JPQO01000157; KGT47507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A3W290; -.
DR STRING; 1509403.GW12_14190; -.
DR PATRIC; fig|1509403.3.peg.1403; -.
DR eggNOG; COG1086; Bacteria.
DR Proteomes; UP000032870; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd05237; UDP_invert_4-6DH_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003869; Polysac_CapD-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43318:SF1; POLYSACCHARIDE BIOSYNTHESIS PROTEIN EPSC-RELATED; 1.
DR PANTHER; PTHR43318; UDP-N-ACETYLGLUCOSAMINE 4,6-DEHYDRATASE; 1.
DR Pfam; PF02719; Polysacc_synt_2; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 276..561
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
SQ SEQUENCE 607 AA; 67661 MW; 05794F065E880A62 CRC64;
MPRHQKQIVL VAMDICVLPV IMWLVYAIRL ARPNVSVMGG LEFWYLYVGV FGVLIFALMG
IYSAIVRSFN EDYLLRLSIA TFIQIVVLYA VKKLDLAFIP MSIPLMYGFV LFSWMWWSRA
LIRYLTLRTF AKKANRKRVA IYGAGLAGQQ IAAALFRSDN YLPVCFIDDK TSLQGQSLSG
LKIYAPKRVL GKFRKFHIEE ILLAMPSVGR ARKKEIIESF EQSDVKIMEL PGVTQLVDGQ
VKVSDIREVD IIDLLGRDPV PPKPELLEKN IKNKVVMVTG AGGSIGSELC RQIVKHQPKL
LVLFEMSEFA LYSIDRELQS PGVKVVPILG SVTNQTKLER VLAQYQVQTV YHAAAYKHVP
LVEANPFEGI YNTSIGTARS VDAAVNQGVE TFVLISTDKA VRPTNVMGAS KRMAELYCQG
LAATKPQTQI SIVRFGNVLG SSGSVVPLFK KQIAHGGPVT VTHPDVTRYF MTIPEAAQLV
IQAGAMGTGG DVFLLDMGEP VKIVDLAKQM IRLSGLRPID ENGVGDIEIQ FTGLRPGEKL
YEELLINAEG VKSTEHQRIL KSFEKYFDFS IISNVFVIFV NIINQQKIED LISILKEYVD
GYSQSKE
//
