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Database: UniProt
Entry: A0A133XF41_9RHOO
LinkDB: A0A133XF41_9RHOO
Original site: A0A133XF41_9RHOO 
ID   A0A133XF41_9RHOO        Unreviewed;       231 AA.
AC   A0A133XF41;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Biosynthetic peptidoglycan transglycosylase {ECO:0000256|HAMAP-Rule:MF_00766};
DE            EC=2.4.1.129 {ECO:0000256|HAMAP-Rule:MF_00766};
DE   AltName: Full=Glycan polymerase {ECO:0000256|HAMAP-Rule:MF_00766};
DE   AltName: Full=Peptidoglycan glycosyltransferase MtgA {ECO:0000256|HAMAP-Rule:MF_00766};
DE            Short=PGT {ECO:0000256|HAMAP-Rule:MF_00766};
GN   Name=mtgA {ECO:0000256|HAMAP-Rule:MF_00766};
GN   ORFNames=AT959_16695 {ECO:0000313|EMBL:KXB29580.1};
OS   Dechloromonas denitrificans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=281362 {ECO:0000313|EMBL:KXB29580.1, ECO:0000313|Proteomes:UP000070186};
RN   [1] {ECO:0000313|EMBL:KXB29580.1, ECO:0000313|Proteomes:UP000070186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-841 {ECO:0000313|EMBL:KXB29580.1,
RC   ECO:0000313|Proteomes:UP000070186};
RA   Yoon S., Nissen S., Park D., Sanford R.A., Loeffler F.E.;
RT   "Nitrous oxide reduction kinetics distinguish bacteria harboring typical
RT   versus atypical NosZ.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Peptidoglycan polymerase that catalyzes glycan chain
CC       elongation from lipid-linked precursors. {ECO:0000256|HAMAP-
CC       Rule:MF_00766}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.1.129; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00766};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00766}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00766}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00766}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 51 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00766}.
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:KXB29580.1}.
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DR   EMBL; LODL01000035; KXB29580.1; -; Genomic_DNA.
DR   RefSeq; WP_066885478.1; NZ_LODL01000035.1.
DR   AlphaFoldDB; A0A133XF41; -.
DR   STRING; 281362.AT959_16695; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000070186; Unassembled WGS sequence.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   HAMAP; MF_00766; PGT_MtgA; 1.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR011812; Pep_trsgly.
DR   NCBIfam; TIGR02070; mono_pep_trsgly; 1.
DR   PANTHER; PTHR30400:SF0; BIOSYNTHETIC PEPTIDOGLYCAN TRANSGLYCOSYLASE; 1.
DR   PANTHER; PTHR30400; MONOFUNCTIONAL BIOSYNTHETIC PEPTIDOGLYCAN TRANSGLYCOSYLASE; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW   Rule:MF_00766};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00766};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00766};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00766};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00766};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00766};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00766}; Reference proteome {ECO:0000313|Proteomes:UP000070186};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00766};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00766};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00766}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00766"
FT   DOMAIN          58..225
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
SQ   SEQUENCE   231 AA;  26560 MW;  65BF1005F29DD5D8 CRC64;
     MKTLGRWLKW AVLGLFGVFL LWQLWLFCWV LLWGWFNPGT TRFMEIRLGE LRQKNPEAQL
     KQQWVPYERI SIHLKRAIIA AEDAKFVDHE GFDWEGMQKA LEKNRKKGRF VAGGSTISQQ
     LAKNLFLTPS KSYFRKVEEA IITVMLENLW SKRRIFEVYL NVIEWGNGVF GAEAAARHYY
     NASAAQLGPE QAARLAGMVP NPRFYDRNRG APGLGRKTSI ILGRMASAEV P
//
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