ID A0A222XAU4_9CELL Unreviewed; 821 AA.
AC A0A222XAU4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glycosyl transferase {ECO:0000313|EMBL:ASR56007.1};
GN ORFNames=CBP52_13930 {ECO:0000313|EMBL:ASR56007.1};
OS Cellulomonas sp. PSBB021.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2003551 {ECO:0000313|EMBL:ASR56007.1, ECO:0000313|Proteomes:UP000214627};
RN [1] {ECO:0000313|EMBL:ASR56007.1, ECO:0000313|Proteomes:UP000214627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB021 {ECO:0000313|EMBL:ASR56007.1,
RC ECO:0000313|Proteomes:UP000214627};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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; CP021430; ASR56007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222XAU4; -.
DR KEGG; cez:CBP52_13930; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000214627; 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 CDD; cd06577; PASTA_pknB; 1.
DR Gene3D; 3.30.10.20; -; 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 InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
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; PF03793; PASTA; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51178; PASTA; 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 Transferase {ECO:0000313|EMBL:ASR56007.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 56..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 717..779
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..804
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 821 AA; 87208 MW; 2B677BF8DA5F9CC3 CRC64;
MAGSSRASSR SRRSTPRGSR ARSTSAGSAG TRKRKFFDYP RSGYTGLHRW LPSWRFMLGS
FLSGVFLVAG AVVAAYATID VPKPGEDVQA QTTTVYYADG STVLGTFAVQ KREIVELDTL
PEWVGNAVVA AEDRTFYDNK GVSLTGMARA FLNNVRGGDK QGGSTLTQQY VERYYVDKTT
TDYVGKFREV LLAVKITNQE SKPEILGRYL NTIYFGRDSY GIQAAAQSYF GVDAKDLTIS
QAAMLAAIIP SPNNWDPAVR PQQAQARWQI VIDRMLEDGH ITKKQHDEAA FPETVEYVRS
SKYEGPDGHL LKMVEDEMAG EAINISKEKL DRGGYKVVTT IQKPVQDQLL TSVGRLLKGE
LTDGETPPSP NLKIAASSVD PATGGVVALY GGPDFLTDQI NWATYGDGVQ AGSTFKPFTL
VAALQSGISL DKRYSGRSPM TLDGWGDGDK QVTNFGGTSY GTMDLVDATA DSVNTVYAQL
NLEVGADKTA AVANAAGVTT PVQDNPANVL GSATVHPLDM ASAYATFAAQ GVHHDAHVVA
KVLNANGSVN YETDGNPERR FEQDVMADAT YAMTQVVERG SGEPYIKPLG VPVAGKTGTS
TGNISAWFVG YTPTLATSVA LSQVGDDGRS WNSITPFGPS PWGGKLVEVT GASIPAHLWA
DYMGPVLQME QFAKERDFPP RADVGDKPTQ RPTTTPSPTP TPTTAPTTEP TQDATAKVPY
RLQGKTQGDA TAALLAVGLE PVIVTKPSDD VAAGRVISVD PAAGTRLPVG SQVTLVVSSG
PKPQPTKKPD PKPDPTPTQT PAPTEAPPAQ EEEGGGDGGG A
//
