ID Q87XI7_PSESM Unreviewed; 1045 AA.
AC Q87XI7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=PSPTO_4191 {ECO:0000313|EMBL:AAO57647.1};
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO57647.1, ECO:0000313|Proteomes:UP000002515};
RN [1] {ECO:0000313|EMBL:AAO57647.1, ECO:0000313|Proteomes:UP000002515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515};
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.,
RA Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B.,
RA Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V.,
RA D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S.,
RA Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B.,
RA Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; AE016853; AAO57647.1; -; Genomic_DNA.
DR RefSeq; NP_793952.1; NC_004578.1.
DR AlphaFoldDB; Q87XI7; -.
DR STRING; 223283.PSPTO_4191; -.
DR DNASU; 1185871; -.
DR KEGG; pst:PSPTO_4191; -.
DR PATRIC; fig|223283.9.peg.4298; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_012369_0_0_6; -.
DR OrthoDB; 8552189at2; -.
DR PhylomeDB; Q87XI7; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
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; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
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:UP000002515};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 160..362
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1045 AA; 116830 MW; BB90A38BA80AF840 CRC64;
MTGLSTMGVF RHSDSKQETL SADRQDDPRT PKRPRRKRYG WRVFWVIVVL ACIALGVAIT
VESRSSRLQA REFSRFAASL RYSMQPGPSS EVVYPGDGPF DKRLGYSSLD EFLPRLLKRD
YVITRQTRFS PDLMRYVQHG FFVPYEEKTQ AGLSITDCRG APLYEFRYPQ QFYATFASVP
PLLVHSLLFI ENRDLLDPQQ PLANPAVDWP RFVKAAWSQV AKMFALPGQS AGGSTLATQL
EKYRHSPDGL TQSGSEKLRQ MISASVRAYQ PGAETLEVRQ RVVRDYLNSV PLSAVPGHGE
VHGLAEGLRV WFGVDFARTN QLLASGPTDQ QGLADKALAL REVLSLVIAQ RRPSHYLAKG
RTELAELTDS HIRLLAQANI IDPPLAEAAL AAKVTYRDWA QQPTLQPIET NKGISVARTR
LSNLLNRPLY DLDRLDLSAT STLHGDLQRS VSQYLRDLAD PEFAAKVGLL GERLLTPAST
TQVRYSFTLF ERGVDGSRVR VQTDSTDQPF DINEGSKLEL GSTAKMRVLT TYLEIIAELH
GRYAGMSTAE LRKVTVEEPD RLTRWAVDYL LLNKDRDLAK MLSAALDRTY SASPAEAFFT
GGGLHRFNNF RREDNERIPT LRESLRESIN LPFIRLMRDV VRYSTYQAPN NSAALLKDDD
DPRRQEYLSQ FADREGTVFL LRFWKRYKDK TTQERLDTFL DGIHPTAIRL AAVHRYLLPG
ADQATFNTFV RAHLEEPKAT STLTDKRLTD LYQSYGPGAY NLPDQGYIAR VHPLDLWLVG
YLLKHPDAQF KDAAAASRFE RQEVYGWLFK SRHKGARDSR VRTMMEVEAF LDIEQRWQRV
GYPFDHLVPS LATAIGSSGD RPAALAELIG IIQNDGIRLP PVRIDSLHFA ADTPYDTELI
INPELGQRVL PSEVATAMRE ALSQVVDGGT AKRVQGTFKM QDGSVLAMGG KTGTGDNRIE
SIGAGGRILS SRAINRTATF VFYIGDNHFG ALTAFVPGRA AEGFRFTSAL PVQVLKGMAP
ILTPYLENHG QAMCNAPLAD PPTGA
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