ID A0A024HIW2_PSEKB Unreviewed; 743 AA.
AC A0A024HIW2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Cellulose synthase catalytic subunit [UDP-forming] {ECO:0000256|ARBA:ARBA00018714, ECO:0000256|RuleBase:RU365020};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539, ECO:0000256|RuleBase:RU365020};
GN Name=bcsA {ECO:0000313|EMBL:CDF84393.1};
GN ORFNames=PKB_3046 {ECO:0000313|EMBL:CDF84393.1};
OS Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1301098 {ECO:0000313|EMBL:CDF84393.1, ECO:0000313|Proteomes:UP000025241};
RN [1] {ECO:0000313|EMBL:CDF84393.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF84393.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Linke B.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDF84393.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF84393.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Miyazaki R., Bertelli C., Falquet L., Robinson-Rechavi M., Gharib W.,
RA Roy S., Van der Meer J.R.;
RT "Genome sequence of the 3-chlorobenzoate degrading bacterium Pseudomonas
RT knackmussii B13 shows multiple evidence for horizontal gene transfer.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of cellulose synthase. It polymerizes
CC uridine 5'-diphosphate glucose to cellulose.
CC {ECO:0000256|RuleBase:RU365020}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-
CC COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000122,
CC ECO:0000256|RuleBase:RU365020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU365020};
CC -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005186, ECO:0000256|RuleBase:RU365020}.
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 glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739}.
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DR EMBL; HG322950; CDF84393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024HIW2; -.
DR STRING; 1301098.PKB_3046; -.
DR KEGG; pkc:PKB_3046; -.
DR PATRIC; fig|1301098.3.peg.3074; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_011907_5_0_6; -.
DR OrthoDB; 9806824at2; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000025241; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR CDD; cd06421; CESA_CelA_like; 1.
DR Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1.
DR InterPro; IPR003919; Cell_synth_A.
DR InterPro; IPR005150; Cellulose_synth.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009875; PilZ_domain.
DR NCBIfam; TIGR03030; CelA; 1.
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; PF03552; Cellulose_synt; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF07238; PilZ; 1.
DR PRINTS; PR01439; CELLSNTHASEA.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF141371; PilZ domain-like; 1.
PE 3: Inferred from homology;
KW c-di-GMP {ECO:0000256|ARBA:ARBA00022636, ECO:0000256|RuleBase:RU365020};
KW Cell inner membrane {ECO:0000256|RuleBase:RU365020};
KW Cell membrane {ECO:0000256|RuleBase:RU365020};
KW Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916,
KW ECO:0000256|RuleBase:RU365020};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU365020};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365020};
KW Reference proteome {ECO:0000313|Proteomes:UP000025241};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365020};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365020};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365020}.
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 60..77
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 84..102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 114..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 425..454
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 484..506
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT TRANSMEM 558..577
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365020"
FT DOMAIN 164..333
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 581..677
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
FT REGION 724..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 82778 MW; 886734D3A239D715 CRC64;
MNSAVQLPRA PDAGRADARL DAWSERLKDC PRWMRLGLIG GGSLLAAALL FCAISAPLDL
ASQSFFAVLC FGSALLIRRL PGRLPILALI VLSLVASLRY MYWRLTATLG FDTWLSAFFG
YGLVAAEFYA LVVLVFGYVQ TAWPLRRRPQ LMQGDPAEWP TVDVFIPTYN EALSIVKLSI
FAAQAIDWPK DKLRVHVLDD GRREEFRDFC RRIGVNYLTR GDNKHAKAGN LNAALKVTDG
EYVAIFDCDH VPTRSFLQIG IGWFLRDPKL AMLQTPHFFF SPDPFEKNLD TFRAVPNEGE
LFYGLVQDGN DLWNATFFCG SCAILRRSTL EEVGGVAVET VTEDAHTALK LNRAGYNTAY
LAIPQAAGLA TESLSRHIAQ RIRWARGMAQ IFRTDNPLLG KGLNIGQRIC YANAMLHFFY
GLPRLVFLTA PLAYLVFGAE IFHASALMIS AYALPHLFHA NLTNSRIQGR FRHSFWNEVY
ETVLAWYIMP PVLMALVNPK FGGFNVTDKG GIIDREFFDW KLARPYIILL LVNLAGLACG
IQQLVWGDPA TRTTVLINLA WTLYNLVITS AAVAVASETR QVRAEPRVRA TLPIRVTLAD
GRQMFCQTQD FSQSGLGLRL PEDTHLDYGE AIRVSLFRNN KSCDFDATVV FSKGNLIGAQ
FAPLTLRQQS ELVRLTFARA DTWAETWGNG KHDTPLAALR EVSSIGWGGL LSLLQATLSL
SRERAKRAKN TSSKPLETLP DPS
//
