ID A0A179DHU7_9SPHI Unreviewed; 796 AA.
AC A0A179DHU7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 18-JUN-2025, entry version 35.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=A5893_06820 {ECO:0000313|EMBL:OAQ40647.1};
OS Pedobacter psychrophilus.
OC Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
OC Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1826909 {ECO:0000313|EMBL:OAQ40647.1, ECO:0000313|Proteomes:UP000078459};
RN [1] {ECO:0000313|EMBL:OAQ40647.1, ECO:0000313|Proteomes:UP000078459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 8644 {ECO:0000313|EMBL:OAQ40647.1,
RC ECO:0000313|Proteomes:UP000078459};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAQ40647.1, ECO:0000313|Proteomes:UP000078459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 8644 {ECO:0000313|EMBL:OAQ40647.1,
RC ECO:0000313|Proteomes:UP000078459};
RA Svec P.;
RT "Pedobacter psychrophilus sp. nov., isolated from Antarctic fragmentary
RT rock.";
RL Submitted (JUN-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAQ40647.1}.
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DR EMBL; LWHJ01000022; OAQ40647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A179DHU7; -.
DR STRING; 1826909.A5893_06820; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000078459; Unassembled WGS sequence.
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:InterPro.
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:UP000078459};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..222
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 305..585
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 703..780
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 796 AA; 90415 MW; 01152D840298834E CRC64;
MQFNKISKKR KIIFLAIFSF LLMWFWFSLP KPLFKSPTSY VIEADNGELL SASIAKDGQW
RFPLNDTVPD KFIKCITTFE DKRFFYHPGV DPFSFTRAVI QNIKNKKVVS GGSTLTMQVI
RLSRNKKRTF YQKVIEIILA FRLELTFSKK EILSLYAANA PFGSNVVGLD AAAWRYFGRN
AKQLSWAETA TLAVLPNAPS LVHPGKNREI LLSKRNSLLE KLFQEKIIDK NTKDLAELEP
IPLEPVSLPT NAPHLLNRFK ADFNDKDFKS TRIKTTLKAN LQLNVSSILK RYHQQFKANG
INNAAALVLD VKTGNTLAYV GNVYEPSDPE MESHVDMIGA LRSPGSTLKP LLYASMMTDG
FLLPNTLIAD VPTQIGGYTP QNYDLGYDGA VPASKALSRS LNIPAVKMLQ KYKYERFYSQ
LKKVGIHSLT NPPDFYGLSI ILGGCEVSIW ELAGAYASIA RSLNHYSQHP NQYDPADYHE
PNYIKQKIQK KENLEKSSVA DYGSLYYTFI AMQEVMRPGE ELLWEQFSSS KKIAWKTGTS
FGFRDGWAIG LTPDFVVCVW VGNADGEGRP NLTGIQTAAP ILFDIFDLLP EKREFTIPYK
NLVKTDVCKI SGFRAGEYCK KKTTYMPLTA LKTEICPYHQ LIHLDHSQKY QVTSACESPE
LMVHKSWFVL PPSMEYYYKV RNRDYQTLPP ISPNCINESD NLRTMELIYP KNNALVYIPL
EIDGQRGKVI FNAAHRNQKS KIYWSIDNEY ITTTQDFHQI AVSPKAGKHT LTLVDDEGNR
LVQIFTVLDK IKKSVK
//
