ID A0A0W7Y3A5_9BACI Unreviewed; 882 AA.
AC A0A0W7Y3A5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=AK833_19615 {ECO:0000313|EMBL:KUF29268.1};
OS Lysinibacillus sp. F5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1700846 {ECO:0000313|EMBL:KUF29268.1, ECO:0000313|Proteomes:UP000053086};
RN [1] {ECO:0000313|EMBL:KUF29268.1, ECO:0000313|Proteomes:UP000053086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F5 {ECO:0000313|EMBL:KUF29268.1,
RC ECO:0000313|Proteomes:UP000053086};
RA Chan X.Y., Chan K.G., Hong K.W., Tan A., Chen J.W.;
RT "Draft Genome of marine Lysinibacillus sp. F5.";
RL Submitted (OCT-2015) 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:KUF29268.1}.
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DR EMBL; LKIE01000094; KUF29268.1; -; Genomic_DNA.
DR RefSeq; WP_058845085.1; NZ_LKIE01000094.1.
DR AlphaFoldDB; A0A0W7Y3A5; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000053086; 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 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 708..806
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..830
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 96881 MW; C00DA5E7E101A3F6 CRC64;
MTERRRTRGE HQKALAEKNK KGKKKTTSSS PAKTWFKRIF LTLLAIGVAG FIGGAGLFAY
YASTAPELDE ELLKDPVSSE FYDKNGELFA TIGAENRKYI KYEDIPEDMV NAILATEDVR
FFEHHGMDFY RLGGAILANF RDGFGAQGAS TLTQQVVKNS FLQNEKKLKR KAQEAWLAFQ
LERKYSKEEI FEMYFNKMLM SGRIYGFGTA AQYFYGKELK DLTLDEEALL AGLVQRPNAY
NPLKNPELAK KRRNTVLGLM HQHGKITKAE MEEAKQMEVQ SGLADDATRQ SFAGSKYDAF
LDIVINELEN NGDGTAMAEG IKVYTTLDPN AQQVVENVMN DDSNFPTEEI QSGVAVIDTK
TGAIQAVGGG RHYGAERGFN YADDLTKNQP GSTMKPLVDY GPAIEYLKWS TGQTLVDEPM
NYTNSKQTIT NWDGRYMGAM TARKALYASR NVPAVKTLQE VGTDKAKEFV GRLGIETENL
YESDAIGGGA ITISPIQMAA SYAAFGNNGV YTDPHAITKI VYRDGKTSKN YTPEPKVAMS
DYTAYMVTDM LRDVVGNKPD ASGTAANVPG LDIAGKTGTT NYSAEDFSKY NLPNTSVPDS
WFAGYTTNYS IAIWSGYEKH FDPITTWEER RLPQNLFKSI MQDISSNVEN TSFKKPNTVV
EATIEVGSKP LKLASDYTPS ELRQTELFVR GTEPTEVSSV YEAPELSTPY NVSASLDLGA
QSINISWEHD AILDPKTDEP LPTSFEVTAK RDGGESITLG TTDSKGLTVG NTLEDGNYTI
SVVAIVDGTR SEPGTTTFQI TSTPEEDLET EDPDEPEIDL PTDPGQEDND NGNDDNGNNN
NNNGNGQGNN GNGSNSGNND GNQQPTPPTE PTNPIEEDQS SE
//
