ID A0A1G8WX17_9BACI Unreviewed; 998 AA.
AC A0A1G8WX17;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05216243_1046 {ECO:0000313|EMBL:SDJ82938.1};
OS Sediminibacillus albus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Sediminibacillus.
OX NCBI_TaxID=407036 {ECO:0000313|EMBL:SDJ82938.1, ECO:0000313|Proteomes:UP000198694};
RN [1] {ECO:0000313|EMBL:SDJ82938.1, ECO:0000313|Proteomes:UP000198694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6502 {ECO:0000313|EMBL:SDJ82938.1,
RC ECO:0000313|Proteomes:UP000198694};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNFL01000001; SDJ82938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8WX17; -.
DR STRING; 407036.SAMN05216243_1046; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000198694; 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:UP000198694};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 695..789
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 549..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..849
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..879
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 998 AA; 109500 MW; 41EF5A3ED5A31B20 CRC64;
MKDYNTRIEK RKKKPLWRKL LFSIIMLGFV ALLAGGGLFT YYASQAPPLE EEELKDPIAS
QILDMNGEVV ASVGTKKRQL VNYEDIPSLV EDAVLATEDV RFYDHFGLDP KRLGGAVLSN
ITEGFGSEGA STLTQQVVKR SFLTSEKSLD RKSQEAWLAV KLEKEYSKEE IFEMYVNKIY
YSDNIYGIAT AADYYFDKSL EDLSLAQAAL LAGMPQSPNS YNPYDHPKRA KERRNTVLAL
MEQHGKISHE EQMKASEIPI TEGLVERSEG ERTYLTGEKK YEAFVDIVIS EVEALGDYNI
YEDGLRIHTT LDPEAQNTME KMLNNDDIIK FPKDKDGQPF QAGVTLLDTN SGAIRAVGGG
RNYGKEAKRG FNFATDTDRQ PGSVIKPILA YGPAIEFMQW STAHIVEDEE FEYENGGKPK
NWDGEFKGPM TIREALLGSR NIPAIKTFNE VGHKKAADFA SNLGLNLEEP LHESAAIGGL
SQGTNPLEVA GAYAAFGNGG TYNEPYAVTK IELRDGSIIE PDHESHQAME NYTAYMVTDM
LKDVLEHPEG TGSQARIPGL PAAGKTGTTN YSEDTLEEYN IDERNAPDSW FAGYTTNYTA
AVWTGYQERK NYLTPEERDT AEKIFKHLME QVSKKSKTKD FEQPDSVVEV EIEDGTDPPK
LASSFTPEEE TSTELFVKGR EPSEESRDFV PDLPAPSGLT TNYDRENEMV LLDWEYSQAD
NDDRKVSFKV TVSSDGQGSE PAGKTEEQEL RIDGIKPGNE YTFTVTAIAD DEQSDPASIV
LQTEQQQPDG STESENESAD TSDSGSETNQ ENNSSNEDEQ TSADDGEENT NQDGQDTADE
EDAQQEQEAN TSSEDDTSNQ EENNEENTND EEGSADDANQ EASSEDSGQT DDSSSSNTGQ
TDESGQESND NEDQSESGSD GNTSSEQSGN NETASGNEES SSNSDDQATS QTESDNSDTG
NNQESDNSSA NDDAGNGSSG DNTGNSSSSD GNSAEDNA
//
