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Database: UniProt
Entry: R4YNZ9_OLEAN
LinkDB: R4YNZ9_OLEAN
Original site: R4YNZ9_OLEAN 
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
//
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