ID A0A380BN24_SPOPA Unreviewed; 867 AA.
AC A0A380BN24;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=ponA_2 {ECO:0000313|EMBL:SUJ02897.1};
GN ORFNames=NCTC4822_01320 {ECO:0000313|EMBL:SUJ02897.1};
OS Sporosarcina pasteurii (Bacillus pasteurii).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1474 {ECO:0000313|EMBL:SUJ02897.1, ECO:0000313|Proteomes:UP000254519};
RN [1] {ECO:0000313|EMBL:SUJ02897.1, ECO:0000313|Proteomes:UP000254519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822
RC {ECO:0000313|Proteomes:UP000254519};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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};
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DR EMBL; UGYZ01000002; SUJ02897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380BN24; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000254519; Unassembled WGS sequence.
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 CDD; cd00063; FN3; 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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR013783; Ig-like_fold.
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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF29; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS50853; FN3; 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 Reference proteome {ECO:0000313|Proteomes:UP000254519};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 680..775
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..796
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..867
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 95860 MW; 26B859623DD90E52 CRC64;
MSDQINSRTE RRRAQQQNNK NQKPRNNKGL IKKIFLALVA IGFIGLISGL GLFAFYASSA
PKLDEELLRD PLSSEILYAN GELMYTTGSE KREYVNYEDI PKLMEDAILA TEDVRFYKHH
GMDFYRLGGA VIANFKRGFG SEGASTLTQQ VIKNSFLTHD KTLKRKAQEA WLAFQLERNY
EKEEIFEMYF NKILMSGNQY GFGTAADYFY GKKLDELELH EVAMLAGLPQ SPNGYNPYNN
PERAEKRRNI VLSLMHQHKK ITKEEMEAAQ ATDVTSTLRP EEERVANNFK YPILLDVVLN
ELEQAGYGDI INDGVQIHTT FNPSAQRIVE ESINNPSIYV DDKIQSGMTV LDTQTGGIVA
IGSRDYSYGT NFARQEKRQL GSTMKPILSY GPAIEYLNWS TGQVVVDEPY KYPNGKSLGN
AYPGFKGPMT IREGLYQSSN VTAVKTFKEV DKNDAMSFAA KLGIKLGDAH EASALGGTTE
EFSTVDLAGA YAAFGNNGVY TKPYSINKIV MRDGKTEKNL KPKSVVAMKD STAYMITDML
RDVFTKPGAT GQNANVPGLD IAGKTGTTNE ARDSWFVGYS TRYTVAAWGG YKDRTPMTSW
QGQRMIPRDL FKGVMKDISA NIETPRFQKP SSVEEVEVVY LSNPLMKASP AIPASMKRTE
LFVKGSVPQE VAKPEVVLNA PSNLSATFNE ENESITLTWE HESPDSELIE GDVEFIVSAN
IDGGETIEVA RTKEFALAFT DVNRGSTYTF SVVASVGELK SDAISTTLKV DGEEEVIPEE
EPEEEPETNP DEENTPPEED NNGKSPGEDG NQGNNGNNGD NGNNGNNGSQ GNSGNNNEGN
REDEEQGADT GTPPDDEIND ENEDEQP
//
