ID K8MVE0_9STRE Unreviewed; 744 AA.
AC K8MVE0;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=HMPREF9186_01134 {ECO:0000313|EMBL:EKS18018.1};
OS Streptococcus sp. F0442.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=999425 {ECO:0000313|EMBL:EKS18018.1, ECO:0000313|Proteomes:UP000001140};
RN [1] {ECO:0000313|EMBL:EKS18018.1, ECO:0000313|Proteomes:UP000001140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0442 {ECO:0000313|EMBL:EKS18018.1,
RC ECO:0000313|Proteomes:UP000001140};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Blanton J.M., Baranova O.V.,
RA Mathney J., Dewhirst F.E., Izard J., Tanner A.C., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. F0442.";
RL Submitted (APR-2012) 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=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
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:EKS18018.1}.
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DR EMBL; AGZZ01000011; EKS18018.1; -; Genomic_DNA.
DR RefSeq; WP_009731837.1; NZ_KB373314.1.
DR AlphaFoldDB; K8MVE0; -.
DR STRING; 999425.HMPREF9186_01134; -.
DR PATRIC; fig|999425.3.peg.1133; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_2_9; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000001140; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 6.20.370.110; -; 1.
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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR NCBIfam; NF038276; strep_PBP2A; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF32; PENICILLIN-BINDING PROTEIN 2A; 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 Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 117..283
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 384..660
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 27..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 81399 MW; DDF4B9A1566A48F9 CRC64;
MKRIKELFEN AITFFRKDHP PKTVAEEVPD TELPEEAVET TYSRSGKHRS KPLSQHPFRR
FWRRFHLTKI LLIIGLGFSL LTGGYLFYLA KTTNVKDLQN ALKATTIIYD KNGDQAGSLT
GQKGTYVELD AISENLQNAV VATEDRSFYK NSGINYGRFF LAILTLGRSG GGSTITQQLA
KNAFLSQDQT VERKAKEFFL ALEINKKYSK KEILTMYLNN AYFGNGVWGI EDASKKYFGV
SASQLSLDQS AVLAGMLKGP EIYNPLYSVE NATNRRNTVL QNMVAAGYID QATADQSAAV
DIHGQLVDAY EGKSEDYRYP SYFDAVINEA VNRYGLTEED IVKNGYRIYT ELDQNYQASM
QVIYDNTALF PVAEDGTRAE SGSVALDPKT GGVRALVGRV GSDENPGFRT YNYATQAARS
PGSTIKPLVV YSPAVAEGWS TNKELDNSTT QYGSYEVNNY AGIQSSPTVP MYQALAESLN
LPAVATANDL GLNTVFEYGK KFGLNMDKVE KSLAVALGAG VTTNPMQMAQ AYGTFANGGV
MNDAHLITKI ENASGQVVKS HSQKSTRVLS GSATDKMTNM MLGTFSNGTG VNAAPYGYTM
AGKTGTTETS FNKDLSGDQW VIGYTPDVVI SQWLGFPTTD EGHYLTDSSA GTASEIFRNV
ANSVLPYTDG TQFDSVKNSY AENGIAPVGE ENTETDTKED KGFFEEVKEK ATNMVDDAKK
AIDEADIPGK AKNAWDTFKG WLGF
//
