GTFA_LIMR5
ID GTFA_LIMR5 Reviewed; 512 AA.
AC A0A0S4NM89; F8KEI5;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit {ECO:0000255|HAMAP-Rule:MF_01472};
DE EC=2.4.1.- {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:30371779};
DE AltName: Full=Glycosyltransferase GtfA {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000303|PubMed:30371779};
GN Name=gtfA {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000303|PubMed:30371779};
GN ORFNames=LRATCC53608_1098;
OS Limosilactobacillus reuteri (strain ATCC 53608) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=927703;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53608;
RX PubMed=21622738; DOI=10.1128/jb.05282-11;
RA Heavens D., Tailford L.E., Crossman L., Jeffers F., Mackenzie D.A.,
RA Caccamo M., Juge N.;
RT "Genome sequence of the vertebrate gut symbiont Lactobacillus reuteri ATCC
RT 53608.";
RL J. Bacteriol. 193:4015-4016(2011).
RN [2]
RP FUNCTION, IDENTIFICATION OF CARBOHYDRATE ALPHA LINKAGE, AND PATHWAY.
RC STRAIN=ATCC 53608;
RX PubMed=30371779; DOI=10.1093/glycob/cwy100;
RA Latousakis D., Nepravishta R., Rejzek M., Wegmann U., Le Gall G.,
RA Kavanaugh D., Colquhoun I.J., Frese S., MacKenzie D.A., Walter J.,
RA Angulo J., Field R.A., Juge N.;
RT "Serine-rich repeat protein adhesins from Lactobacillus reuteri display
RT strain specific glycosylation profiles.";
RL Glycobiology 29:45-58(2019).
CC -!- FUNCTION: Required for polymorphic O-glycosylation of the serine-rich
CC repeat protein (SRRP) in this bacteria. Catalyzes the first step in
CC glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to
CC serine residues in the substrate protein. Part of the accessory
CC SecA2/SecY2 system specifically required to export serine-rich repeat
CC cell wall proteins encoded in the same operon. The GtfA-GtfB complex
CC adds GlcNAc from UDP-GlcNAc to SRRP (experimentally characterized with
CC a truncated SSR1 construct); the alpha linkage was shown for this
CC enzyme but not the residues glycosylated on SRRP.
CC {ECO:0000269|PubMed:30371779, ECO:0000305|PubMed:30371779}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-
CC acetyl-alpha-D-glucosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:59872, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15471,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:143279;
CC Evidence={ECO:0000250|UniProtKB:A0A0H2URG7, ECO:0000255|HAMAP-
CC Rule:MF_01472, ECO:0000305|PubMed:30371779};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:30371779}.
CC -!- SUBUNIT: Forms a heterotetramer with 2 subunits each of GtfA and GtfB.
CC Part of the accessory SecA2/SecY2 protein translocation apparatus.
CC {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000305|PubMed:30371779}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01472}. Cell
CC membrane {ECO:0000255|HAMAP-Rule:MF_01472}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01472}. Note=Cell membrane association
CC requires GtfB. {ECO:0000255|HAMAP-Rule:MF_01472}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000255|HAMAP-Rule:MF_01472}.
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DR EMBL; FR854365; CCC03850.1; -; Genomic_DNA.
DR RefSeq; WP_003675577.1; NZ_LN906634.1.
DR AlphaFoldDB; A0A0S4NM89; -.
DR SMR; A0A0S4NM89; -.
DR HOGENOM; CLU_009583_21_0_9; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017122; C:protein N-acetylglucosaminyltransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01472; GtfA; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR014267; GtfA.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR02918; TIGR02918; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasm; Glycosyltransferase; Membrane;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..512
FT /note="UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase GtfA subunit"
FT /id="PRO_0000447248"
FT BINDING 16..19
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472"
FT BINDING 251
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472"
FT BINDING 393..394
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472"
FT BINDING 413..416
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472"
SQ SEQUENCE 512 AA; 59376 MW; 6CD4FC93B9F0B959 CRC64;
MTVYNINLGI GWASSGVEYA QSYRAQAFRN LNISAKFVFS DLILGNNIAD LTANLGFNAD
QIIWLYNFFT DIKIAPSTFL LDTFVEQNHL EQRNFSLLPN NGTKELQYKS EEEKLTIVPR
YNNREKQTID QVTYIFNNRL IKRDFYSYTK YATEYYSGEE KDNQVIFREF YNENGTIAYT
QHLDGDGHEL FEFPDQNYYS KTDLYREMLR KFNFKADDII ILDRMDEDKQ LVNGQLIFEH
HLPAKLVIPV HADHYDKHYT NDHQVLWNNF YEYQFMHYQD VAAYVVATDR QRDLLASQQK
HFNHAKPQIN TIPVGSLEHL VKPKGTRKKH SLITASRLAN EKHIDWVIEA TVAAHKIVSD
LTLDIYGEGG ERSRLQNLIT KNNADSYIKL MGQHDLKDVY QKYETYIAGS TSEGFGLSLM
EAVGSGLSMI GFDVPYGNQT FIVDQQNGYL LPYTEDWSNS RKEQLLADAI VKNFTEADLT
SFHEKSYSLA ESYLTKNVAK QWQQLIGELQ HA
