ID A0A090ZHM2_PAEMA Unreviewed; 1034 AA.
AC A0A090ZHM2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=DJ90_3557 {ECO:0000313|EMBL:KFN09720.1};
OS Paenibacillus macerans (Bacillus macerans).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=44252 {ECO:0000313|EMBL:KFN09720.1, ECO:0000313|Proteomes:UP000029278};
RN [1] {ECO:0000313|EMBL:KFN09720.1, ECO:0000313|Proteomes:UP000029278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8244 {ECO:0000313|EMBL:KFN09720.1,
RC ECO:0000313|Proteomes:UP000029278};
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (APR-2014) 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:KFN09720.1}.
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DR EMBL; JMQA01000021; KFN09720.1; -; Genomic_DNA.
DR RefSeq; WP_036621540.1; NZ_UGSI01000001.1.
DR AlphaFoldDB; A0A090ZHM2; -.
DR STRING; 44252.DJ90_3557; -.
DR GeneID; 77006277; -.
DR PATRIC; fig|44252.3.peg.2052; -.
DR HOGENOM; CLU_006354_2_0_9; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000029278; 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; 2.
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 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; SSF49265; Fibronectin type III; 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 Reference proteome {ECO:0000313|Proteomes:UP000029278};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..280
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 398..662
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 113331 MW; 52A3A77EB3374ADE CRC64;
MVHDNENNSG QQKKRRSKSG KPVRRPRKGR WIWATLGWLV LLGFAGVLFA GGAVFGYVSS
IVKDDPVRSR ADIEAKINYN EMTGFAYFRD GQAIGQLRSE EDRRPVTYQQ IPQSVIDAVI
AIEDNHFNEH IGVDFKGTLR AVKQRLLHES VQTGGSTLTQ QLARRVFLNL ERTEDRKVKE
ILLALRLERF LSKEEIITAY LNKVPFGNGS NGYQVYGIKA AAKGIFNISN LEDLNIAQTA
YLAGLPQLPS SYSAFNGKGE FNEEAFGRAM KRQQLVLQRM LEENKITQAQ YQEALAFDLK
GSLAQQTKKA YDTYPYLMLE TERQGAIVLA MLRNPELTKE QAASRPQILE DARQELLTGG
YKVYTTIDKQ VYNSMHKVSE NADNFSPSSE KKGLEQVAAM MLDNDTGAIL GMIEGRDFYT
EQMNYATQMK RQPGSTMKPI AAYLPALDAG LIQPASIIDD SPIILRDYQK GYHIPVNSSG
GYKGLVTART ALNESRNIPA LKVFNNIVGI DKAWDFAKKL GITTLEDEDY NAQTGVLGGL
KYGVTVEELT NAYSAIPNGG KFVDAYMIEK IVDAKGKVVY KHKNEPKQVF SEQTAYLMTD
MLRTVIRDGT GSSIKRDFKN YGKIPVVGKT GTTQNYADVW FMGYSPDVTL GVWIGYRDSV
NTLSDAGKSR ARKIWSLVMN EVTANEPDLF ATKEFKKPDG IVTKTVSGYS GKLPTQLTQQ
AGKLVTDIFN AKYVPTKSED VLVRAKYVTY DGVNYVPLET TPSDMQREKV VVRREKPIAE
LVKELQNAFS VMKGSHRSLS YYMPRDAGED APYKPDPRTD DGNAPASPGG VALKINGSTA
TVTFGANSEK DVVGYRLYRS DDGVEFQYTG KAALIGDDLS ITDANAAGPA TSYYVTAVDV
AGKESEPSAV VGLLGGINPE GVTPPDSSGE TPEDGGTAGE NGTDGSLPAS PAQVSIKKDE
RGFTASWEAN PALDLVTSYN VYVSDAADGT YSKAGSTADT QYSFKTDSGS VWVKVTAVNV
LGESPASSPV QYSK
//
