ID A0A1L7FGY4_9PSEU Unreviewed; 914 AA.
AC A0A1L7FGY4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-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=UA75_30515 {ECO:0000313|EMBL:APU24066.1};
OS Actinoalloteichus sp. GBA129-24.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=1612551 {ECO:0000313|EMBL:APU24066.1, ECO:0000313|Proteomes:UP000185506};
RN [1] {ECO:0000313|EMBL:APU24066.1, ECO:0000313|Proteomes:UP000185506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GBA129-24 {ECO:0000313|EMBL:APU24066.1,
RC ECO:0000313|Proteomes:UP000185506};
RA Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA Kalinowski J., Zotchev S.B.;
RT "Complete genome sequence of Actinoalloteichus fjordicus DSM 46856
RT (=GBA129-24).";
RL Submitted (JUN-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; CP016077; APU24066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7FGY4; -.
DR SMR; A0A1L7FGY4; -.
DR STRING; 1612551.UA75_30515; -.
DR KEGG; acti:UA75_30515; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000185506; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF34; 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; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:APU24066.1}; 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 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 221..381
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 472..735
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..142
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..842
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 96921 MW; 7341520405AC1C01 CRC64;
MQSPPPQNGD RRPPRQGGPS ALGAAAAGAA LGAAGGAAAA AGMNAGAPPG MGTPPGGVPG
AGAPGGPGPA NGAPPAHTQA LRQGAGTGPR RPGEPSTQMM QPGDEQPTTQ MEPALLTHRE
PAQLEDGYDE DDYYDDEDDA EESPEAVKKA KRKKIWRRVR RTCYVMAGLG ILTPVVAFAV
GYQMWDVQSP EAILADLDKT VTVTYADGSE MLRIVPNGEG EGDRRFLDYE DIPEDFYNGV
TATEDPTFRD NMGFSPVGIV RAAVTGTGGG STITQQYVKL STGNDDGTYA RKFQEVVMAF
KLTQQQDKDY IFESYANLTS FGRNTYGLEA GAQTWFGKSA SELELNESLF LAGILNAPTL
FDPDNNRDGM ENRFAYVVNK MVERDHLSQA EADAVEFPDY LPRGAGGGTG RSITDVHVQT
QIENELTARG IEMDQVRREG MVIRTTIDKT AQEQSEAVMA EHFAGQPDEL RGALVAVDPA
NGAVRAYNGG EWSAGIDFAA AKQPPGSSFK PFVVAAGLKR GQGLGEFYDG RESIDIEGTT
FSNTAQCPTG ANEHCSVRNA MLVSANTPFI DMAHQFGPGS VAEAAWEAGI PEEINGEPTL
VNTEGFTAAG IALGQYEVRT IDMAAAYATF ASGGVRHDPY FVEFVGHEGD GPDDEVLINR
AEEGHEGVQA FGPQSKAVAD NITEVLKPVA ANSGHDLPGR EVAAKTGTHQ FAQSAGNQAG
WMVGYTPQIS VAVWVGSEVP APLTVNATAT NPSTEQLWGR NVPAFSWKAF MEAYLGDKEA
ASFPTDITQI GIFPEQPRPA PPPPPPSPDW DDDRDRDRDE EDGRDEDEEG DEGDENGEGG
EGDDESTPNP PTDTTEPTPT GPDDSCLWPG QCEGEGDGRP GDGRPGDRGT TGFGFSRDDS
RPEVAPTGDV PLPN
//
