ID C5C662_BEUC1 Unreviewed; 836 AA.
AC C5C662;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Glycosyl transferase family 51 {ECO:0000313|EMBL:ACQ82420.1};
GN OrderedLocusNames=Bcav_4182 {ECO:0000313|EMBL:ACQ82420.1};
OS Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Beutenbergia.
OX NCBI_TaxID=471853 {ECO:0000313|EMBL:ACQ82420.1, ECO:0000313|Proteomes:UP000007962};
RN [1] {ECO:0000313|EMBL:ACQ82420.1, ECO:0000313|Proteomes:UP000007962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432
RC {ECO:0000313|Proteomes:UP000007962};
RX PubMed=21304633; DOI=10.4056/sigs.1162;
RA Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT 0122).";
RL Stand. Genomic Sci. 1:21-28(2009).
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; CP001618; ACQ82420.1; -; Genomic_DNA.
DR RefSeq; WP_015884657.1; NC_012669.1.
DR AlphaFoldDB; C5C662; -.
DR STRING; 471853.Bcav_4182; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; bcv:Bcav_4182; -.
DR eggNOG; COG0744; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_006354_6_2_11; -.
DR Proteomes; UP000007962; 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; 2.
DR Gene3D; 3.30.10.20; -; 2.
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; 2.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 2.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51178; PASTA; 2.
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:UP000007962};
KW Transferase {ECO:0000313|EMBL:ACQ82420.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 67..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 678..743
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 765..830
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..766
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 88551 MW; F5F1E6CCAABFEB09 CRC64;
MASAGKRTNA RRSGGGSGGG SNRPSGSGTA RANGARTSSA KPKRKRGWNY PRQGLGPIRR
WLPSWRVLLG TFVTGVALVA GLFAAAYATT DIPERDDLAL AEGSTVYFAD GTTEIGTLAE
VNREIVDTTQ LPDYVGNAVV ASEDRRFYSN SGIDPIGIAR ALWNNLRGGG QQGGSTLTQQ
YVERYYLGTT TDYVGKFREA ILAVKLDREL DKSEILDAYL NTIYFGRNAY GIEAAAQSYF
GKPASELTIS ESALLAGIIP SPNNWDPATN PEQAESRWSR VLDFMVQDGW ITEADRNEAT
FPEVVEYQRS DTFAGPNGYL LQMAIDELTT GDDAPYTVEE LNRQGLAITT TIDPTMQQAA
VDTMQNMVTG YAPELRNTLV SIDPATGGIR ALYGGTDFIA ESYNRATQAV YQGGSTFKPF
TLVAALEQGV TLEDRYESYA PRDIDGWNVR NFDRVNRGSI DLVEATVNSV NTVYGQLNHD
IGPENTRDVA VRAGLPEDTN GLDAVDSNVL GSAAPHAVDM ATAYATFAAQ GERHETHIVE
QVAGREGNVE YTADTTGEQV IDAEVMADAT YAMTQVVERG TGETASQLDR PVAGKTGSSN
DYTAASFAGY VPQLATVVAL YQPGADGEIQ TITPFGGYDP VAGGTVPADL WTQYMQTATQ
GMEVQEFPER STPPPPPPPE MVAVPDVVGL DEATATAQIG EVGLVASVSQ EPSTQPAGTV
VHTDPGAGTE VVVGSTVTLV VSSGPPEPTE EPTEDPTEDP TEEPSDEGVP VPDTTGMEAT
AAQVQLSLAG FTVVRADEAS DQQPAGFVVR QDPAGGTAPR GSTITIVVST GPPDGG
//
