ID A0A1K1RFU2_9GAMM Unreviewed; 788 AA.
AC A0A1K1RFU2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 18-JUN-2025, entry version 32.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=SAMN02800691_3123 {ECO:0000313|EMBL:SFW70550.1};
OS Luteibacter sp. UNCMF366Tsu5.1.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Lysobacterales; Rhodanobacteraceae; Luteibacter.
OX NCBI_TaxID=1502758 {ECO:0000313|EMBL:SFW70550.1, ECO:0000313|Proteomes:UP000182005};
RN [1] {ECO:0000313|EMBL:SFW70550.1, ECO:0000313|Proteomes:UP000182005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNCMF366Tsu5.1 {ECO:0000313|EMBL:SFW70550.1,
RC ECO:0000313|Proteomes:UP000182005};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FPIS01000003; SFW70550.1; -; Genomic_DNA.
DR RefSeq; WP_072323495.1; NZ_FPIS01000003.1.
DR AlphaFoldDB; A0A1K1RFU2; -.
DR STRING; 1502758.SAMN02800691_3123; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000182005; Unassembled WGS sequence.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000182005};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 61..209
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 318..535
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 695..779
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 788 AA; 87053 MW; FA1ABDE392E6D121 CRC64;
MKSFPRLRLP RWHNVLVALL LLAAIPVTCR LWPHDPLRAW FPSSTAVYDA DGHLLRLTLA
SDDRYRLWVP LEDISPAMVE GVLLHEDRWF RWHPGVSVWG LFRGAWMTYV RAGNRQGGST
VTMQLARLIW HLDTRHPRGK LVQMARAVQL ELFYSKHDIL EAYLNAAPYG RNVEGVGAAS
LAYFGKSPAR LSLPEALTLA VIPQDPARGL PGNVNGSAVI DTALKTSRDR LFARWISKHP
DDAAARPLFD LPLRLRPLSR LPFEAPHFVE QVLAERRLDG DDEMRVVTTL DLGLQHSLER
QVRQYVERGA ERGIRNAAAI LVDTRDMGIK AMVGSAGYSD ASIQGQVNGT LAKRSPGSTL
KPFIYALGFD QGVLHPETVL RDVPSAFGPY TPENFDGHFL GPVTATQALV RSRNIPAVQV
AAKLASPNLY QFLRDAGISR MASERHYGLS LVLGGGEVTM QELASLYAML ANRGELRPLR
LLASTPKTRG TRLLSEEASF MVMDMLRQNP RPDDAVAGQP SRLPMYWKTG TSWSFRDAWT
AGSFGPYVLV VWIGNFDGSG NPAFVGVDAA APLFFRIADA LRAERPGLAE PIRRNPPNLR
RVPICLASGD LPNAWCPQVG STWFIPGKSP IRVSNVHRPV VIDTTTGKPA CPPYEPGRTR
VEVYEYWPSD LARVFAQAGM PRRLPPPLPD CQGGGQPAGD PPQITSPLKG SSYRIRMSRL
GDERIAFTAT ADASSRTLYW FVDDAYLGSA ANGQPLMWAP ERTGRFLVRV VDDQGRTDSR
ALDVGAIE
//
