ID A8G3E1_PROM2 Unreviewed; 589 AA.
AC A8G3E1;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=mrcB {ECO:0000313|EMBL:ABV50122.1};
GN OrderedLocusNames=P9215_05061 {ECO:0000313|EMBL:ABV50122.1};
OS Prochlorococcus marinus (strain MIT 9215).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=93060 {ECO:0000313|EMBL:ABV50122.1, ECO:0000313|Proteomes:UP000002014};
RN [1] {ECO:0000313|EMBL:ABV50122.1, ECO:0000313|Proteomes:UP000002014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9215 {ECO:0000313|EMBL:ABV50122.1,
RC ECO:0000313|Proteomes:UP000002014};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000825; ABV50122.1; -; Genomic_DNA.
DR RefSeq; WP_012007255.1; NC_009840.1.
DR AlphaFoldDB; A8G3E1; -.
DR STRING; 93060.P9215_05061; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; pmh:P9215_05061; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_3; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000002014; 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 9..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..231
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 320..545
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 589 AA; 66857 MW; 67D5D9E8F2570182 CRC64;
MQKIKSKYFV LIIPILIFSG ISIYIFSLII TTLKFDIPKN KKSRATKYSY VISSSDDKIL
SKLSHKFEIE NNQNQIPLFL KNAFISSEDK KFYKHNGIDL KSISRAIFQN IRSGYVKEGG
STITQQVARI LFLNNDLKIQ RKIKEIFLSL ILEFKYDKQQ ILKLYLNNIY LGSGAYGVNE
ASQIYFGKLI EELTLSEIAL IAGLAPAPSI YSPYQNIELA IKNRNKVLES MYLDGYISLA
SKNKAIEEKI NLNYQTADKF LDDKLLINFI LEETDRIIAN KNDYKFLNIK SSINKNWQEK
AQSISIYAGP KELEFALLSI ESNTGKIKTM ITSKNPSINE FNRVISSIRP LGSTFKIIPY
AAALIEGIKL SDKFEDLPKC WESYCPKNFS EDYRGSISLL ESFKSSSNIV PISITKKIGL
KNIINLANSF GLGYEQEFEE FPSLAIGSYG DNLLNITNVY SAINNNGKIQ SPEIIEKIES
FKKQTIWENK SISKKILDFK INKKINKLLE KSVKEGTSQA ASIKGKKIYG KTGTSDGNKD
LWFIGSIDNL TTGIWIGYDD NKESELSSGN AAYLWKKFIS EIYKIPIKK
//
