ID R4YNZ9_OLEAN Unreviewed; 781 AA.
AC R4YNZ9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 18-JUN-2025, entry version 46.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=OLEAN_C26600 {ECO:0000313|EMBL:CCK76836.1};
OS Oleispira antarctica RB-8.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Oceanospirillales; Oceanospirillaceae; Oleispira.
OX NCBI_TaxID=698738 {ECO:0000313|EMBL:CCK76836.1, ECO:0000313|Proteomes:UP000032749};
RN [1] {ECO:0000313|EMBL:CCK76836.1, ECO:0000313|Proteomes:UP000032749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23877221; DOI=10.1038/ncomms3156;
RA Kube M., Chernikova T.N., Al-Ramahi Y., Beloqui A., Lopez-Cortez N.,
RA Guazzaroni M.E., Heipieper H.J., Klages S., Kotsyurbenko O.R., Langer I.,
RA Nechitaylo T.Y., Lunsdorf H., Fernandez M., Juarez S., Ciordia S.,
RA Singer A., Kagan O., Egorova O., Petit P.A., Stogios P., Kim Y.,
RA Tchigvintsev A., Flick R., Denaro R., Genovese M., Albar J.P., Reva O.N.,
RA Martinez-Gomariz M., Tran H., Ferrer M., Savchenko A., Yakunin A.F.,
RA Yakimov M.M., Golyshina O.V., Reinhardt R., Golyshin P.N.;
RT "Genome sequence and functional genomic analysis of the oil-degrading
RT bacterium Oleispira antarctica.";
RL Nat. Commun. 4:2156-2156(2013).
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; FO203512; CCK76836.1; -; Genomic_DNA.
DR AlphaFoldDB; R4YNZ9; -.
DR STRING; 698738.OLEAN_C26600; -.
DR KEGG; oai:OLEAN_C26600; -.
DR PATRIC; fig|698738.3.peg.2759; -.
DR HOGENOM; CLU_006354_7_2_6; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000032749; 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 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:UP000032749};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..227
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 306..554
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 692..771
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 781 AA; 87326 MW; 92598919C58FDCF8 CRC64;
MNVKTQSSTV KIIAAVCVAV IFSVLISSWW HSLPQPLFNS PYSSILLDRN NQLLEARIAS
DEQWRFPPSE TLPSSYIKAV LLFEDKRFYT HSGVDFLALG RATLQNIKAK EVVSGASTLS
MQVIRLASDN QSRTLSTKLI ETLQALRLEF SYDKQEILNL YASHAPFGGN VVGISAASWR
YFGRAPESLS WAESALLAVL PNRPNYLRPG KNQQKLKQKR DRLLTRLQQA GEFDQLQLTL
ALSEPLPDKI LAFPKRAPHL LETLISRNFN QAVIKTSLNS NLQAQVQSVT NNYAQRLLNS
QITHLAAVVL DNKSGLPVAY IGNSGFSHNP HSGKGIDLLH RARSTGSILK PLLYATMLQQ
GEITPLQLVE DTPTKFKGYQ PENYDLKFRG VVPAKQALAQ SLNIPAVNML KQYGIKPFYD
FLETRGMSTL HRNADDYGLP LILGGAEGTL WEMTHLYMQL ARAAQSLPAQ AISRLPTIAI
EEPSILDTSH LGAGAAWLTL NALLEVGRPG SESRWRQFSN SRKVAWKTGT SYGFRDGWAI
GTTAEYTIGV WTGNAEGGGV PGLTGTQAAA PLLFELFNLL PKTHWFSKPE YDLRQVRVCK
NDGFLATPYC DSKVIDLPLV SSYSKISPYH MRIHTDAKQH YRVSSACEPV HKLSSLNWFT
LPPHVAFYYQ KQHSEYRPMP KWRQDCLNFM SAQSPISFIY PHKGTQIYLP TTMDGSRTKM
VSELAHQYSA SQVYWYLDQE YLGTTQQIHQ MEIGPGLGKH ELLVVDEAGN QQVLGFEVLS
Q
//