ID Q7V2P5_PROMP Unreviewed; 587 AA.
AC Q7V2P5;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=PMM0427 {ECO:0000313|EMBL:CAE18886.1};
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59919 {ECO:0000313|EMBL:CAE18886.1, ECO:0000313|Proteomes:UP000001026};
RN [1] {ECO:0000313|EMBL:CAE18886.1, ECO:0000313|Proteomes:UP000001026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4
RC {ECO:0000313|Proteomes:UP000001026};
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(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};
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DR EMBL; BX548174; CAE18886.1; -; Genomic_DNA.
DR RefSeq; WP_011132063.1; NC_005072.1.
DR AlphaFoldDB; Q7V2P5; -.
DR STRING; 59919.PMM0427; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; pmm:PMM0427; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_3; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000001026; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UniProtKB-EC.
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 InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..231
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 323..545
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 587 AA; 66807 MW; 2E50D6CD09263C80 CRC64;
MNEIKYKYFI FSSSIFIFFV IFFPIFNLIR ITLNFDPLKI NTSKSIPYSY EIFSSDNKTL
RKLSRKFDVL DNANSIPFFL KYSFISGEDK RFFNHNGIDL IGLSRAFISN IQSGYFKEGG
STITQQVARL IFLNNDLSFQ RKIKEIIISL VLDLKFSKNQ ILKLYLNNIY LGSGAYGINE
ASQVYFGKLI TELSLSEVAL VAGLAPAPSI YSPYENIDLA IKKRNKILKD MYIDGYISLD
ERNEALKEKV NLNYSINNKD SKDNLLVNFI LKETNNKIKN HKKYKFLRIK SSINKDWQEI
GQKISRSIGS NNIETALLSI ESNSGLIRTM ITSKNPTINE FNRVTSAIRP LGSTFKIIPY
TAALKEGIKL RDKFEDLPKC WEDYCPKNFS EIYRGKISLI DSFKTSSNIV PLKISSNIGL
KKIINQANLF GLGYEQPLEE FLPLAIGSYG DSLLNITNAY ATLNSNGNLY KTSILEKIES
NNNELIWENK FIHEKILDSE VNKSLNNLLE KSVSEGTSIA ASIKGERVYG KTGTSDGNRD
LWFIGSINNL TTGVWIGFDE NKETKLSSGN AAYFWKKFIS KIYDLEI
//
