ID Q316S6_OLEA2 Unreviewed; 734 AA.
AC Q316S6;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 18-JUN-2025, entry version 111.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN OrderedLocusNames=Dde_0269 {ECO:0000313|EMBL:ABB37070.1};
OS Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS (Desulfovibrio alaskensis).
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC Desulfovibrionales; Desulfovibrionaceae; Oleidesulfovibrio.
OX NCBI_TaxID=207559 {ECO:0000313|EMBL:ABB37070.1, ECO:0000313|Proteomes:UP000002710};
RN [1] {ECO:0000313|EMBL:ABB37070.1, ECO:0000313|Proteomes:UP000002710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA 1058 / DSM 17464 / G20
RC {ECO:0000313|Proteomes:UP000002710};
RX PubMed=21685289; DOI=10.1128/JB.05400-11;
RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT "Complete genome sequence and updated annotation of Desulfovibrio
RT alaskensis G20.";
RL J. Bacteriol. 193:4268-4269(2011).
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=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR EMBL; CP000112; ABB37070.1; -; Genomic_DNA.
DR AlphaFoldDB; Q316S6; -.
DR STRING; 207559.Dde_0269; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; dde:Dde_0269; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_3_7; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002710; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR050396; Glycosyltr_51/Transpeptidase.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:ABB37070.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002710};
KW Transferase {ECO:0000313|EMBL:ABB37070.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 43..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 99..265
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 341..564
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 645..722
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 78789 MW; 01B74ABAB9B4D843 CRC64;
MPPARIMCNG NPPETDFPMP LTQHQPPATQ HTARTRPALI RPAFIRAAAA VGISLFCTVM
LLLVLDAAFP PDLSRYNRRS VLVTDAEGRL LHAFLSPDGM WRLHTTPHDV DSRYLDMLRT
YEDKRFGMHP GVDPLAVLRA AAQLAVSGHV VSGASTLSMQ AARLLQPRPR TLKAKLTEAL
RAMQLHWRYG SNGVLSIYLT LAPFGSNIEG VRAASLAYFG KEPRRLTTGE AALLVALPQS
PTQLRPDRNP LEARKARDKI LGRMHAAGII SGRQHTEART ESIPAVRRQM PALASVLALN
MRNAAPRREH IATALSLPVQ HAAETLCQRH ALSMEQGAAT AAVVLHRATR QVRAYVGGKN
ADASRNYLDL PRALRSPGST LKPFIYGLAF SEHILHPETL ISDEAHRFGD FSPRNFRRGY
QGAVTVREAL RDSLNVPAVS VLYALGPDRL VAALRNAGAT LAVEGDATLP IALGGAGTTL
LDLTTLYAAL ADGGTALPPQ FVPAVLPAPQ QGFRLMDSAA AWQVIDILKD SPRPQGYLSA
AAGGRPVAFK TGTSYGYRDA WAVGASPDWV VGVWTGRPDG RPRPGAVGRT AAVPLLLDIF
GRLPPDTGPW PSPPAGVLDV RDNRRLPTGL QRFVPGSGTG LPVLAGEPPR ILHPQQGATV
ESLGQQAGEG IALRASGGTA PLRWVVNGLP LPEDQHYWLP DSEGFARLTL VDAAGRSATV
QIRIILPQQP ALAP
//
