ID A0A073J0D6_9RHOB Unreviewed; 659 AA.
AC A0A073J0D6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Curdlan synthase {ECO:0000313|EMBL:KEJ95434.1};
GN ORFNames=SUH3_20835 {ECO:0000313|EMBL:KEJ95434.1};
OS Pseudosulfitobacter pseudonitzschiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudosulfitobacter.
OX NCBI_TaxID=1402135 {ECO:0000313|EMBL:KEJ95434.1, ECO:0000313|Proteomes:UP000027746};
RN [1] {ECO:0000313|EMBL:KEJ95434.1, ECO:0000313|Proteomes:UP000027746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|EMBL:KEJ95434.1,
RC ECO:0000313|Proteomes:UP000027746};
RA Lai Q., Hong Z.;
RT "Sulfitobacter sp. H3 (MCCC 1A00686) Genome Sequencing.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KEJ95434.1}.
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DR EMBL; JAMD01000006; KEJ95434.1; -; Genomic_DNA.
DR RefSeq; WP_037926591.1; NZ_WKFG01000017.1.
DR AlphaFoldDB; A0A073J0D6; -.
DR OrthoDB; 9806824at2; -.
DR Proteomes; UP000027746; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016759; F:cellulose synthase activity; IEA:InterPro.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR CDD; cd06421; CESA_CelA_like; 1.
DR InterPro; IPR003919; Cell_synth_A.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43867; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR PANTHER; PTHR43867:SF2; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR Pfam; PF13641; Glyco_tranf_2_3; 1.
DR PRINTS; PR01439; CELLSNTHASEA.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000027746};
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}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 515..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 659 AA; 73800 MW; 05DF6FB92C84F5AA CRC64;
MVFPHLSEVQ SSVTLLMLLA GVGLILPTVI DRNSTFQRSL VLGLAALLAG RYAFWRITET
VAPFGLTMDM LASWSLLALE MLALVGSMSA FLIMSRQRGR SDEATEHAGW WGEKSPRVAI
LIATYNETLD VLERTVVGAK SLRHDNKEVI VLDDGRRDWL RDYCESQQVR YVRRPDNKGS
KAGNINHTLA LLAADPVPPD FVAVLDADFV PHRGFISRSM ALFHDPTVGL VQTPQHFFNA
DPIQHNLGLS RSYPDEQRFF FDHMQPCRDG WGIAFCCGTS SMVRWSALQE IGGLPTESIT
EDFMLTLTLQ NAGWKSVYLA EPLTEGLAPE GLKEYVTQRA RWCLGLMQIA RSDLGPLGKN
KLRLRDRWSV ADSVFYWLTT FPFRLAAIVY PLLYWFGNVT VVDARLPDVI SYFGAYYLWI
LIVLNTLSRG MVIPILNDVS QLIGAIPISR AAIVGLIKPK GYPFSVTAKG GDRTRIVVQW
SMMAPFAVLL GLTLLGLVIG IFWDRFAFSD AGDGKWVVLF WTIYNLFVLS VAIIACIELP
RRERHVADAP EKARFDTGEK QRDLWIASLK SDTVRLRGHP YAEGTRGRLA IRDVGEVEAY
VIATLADGAR LHLLPTDEQR EALLLRFYAE DNMPGIARVR TAAMLRDIAR RLSFSSDSS
//