ID A0A0A1DQP3_NOCSI Unreviewed; 756 AA.
AC A0A0A1DQP3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Multimodular transpeptidase-transglycosylase {ECO:0000313|EMBL:AIY19679.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:AIY19679.1};
GN ORFNames=KR76_03010 {ECO:0000313|EMBL:AIY19679.1};
OS Nocardioides simplex (Arthrobacter simplex).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Pimelobacter.
OX NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY19679.1, ECO:0000313|Proteomes:UP000030300};
RN [1] {ECO:0000313|EMBL:AIY19679.1, ECO:0000313|Proteomes:UP000030300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY19679.1,
RC ECO:0000313|Proteomes:UP000030300};
RX PubMed=25573942;
RA Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT Ac-2033D.";
RL Genome Announc. 3:0-0(2015).
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; CP009896; AIY19679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1DQP3; -.
DR STRING; 2045.KR76_03010; -.
DR KEGG; psim:KR76_03010; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_6_11; -.
DR Proteomes; UP000030300; Chromosome.
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:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 Glycosyltransferase {ECO:0000313|EMBL:AIY19679.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030300};
KW Transferase {ECO:0000313|EMBL:AIY19679.1}.
FT DOMAIN 664..732
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 715..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..756
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 80132 MW; C1CA4B130DC30F30 CRC64;
MLLVAAVLGV VVAGLAIPFA GVVGFSARNV AESVDDLPQE LETEQLPQRT EIEDINGKTI
ATLYDQNRVN VPLRQISRTM VEAIVAIEDF RFYQHGALDL KGTMRALLTN QASGGVAQGG
SSITQQLVKL TLLNQADTDE ERKAATDDTY GRKLRELRYA IALEKRHSKD WILERYLNTA
YFGDGAYGVQ AAAQHYFSVN AKDLNLRQAA LLGGLVQSPE AYNPTKNPAQ ATVRRNIVLD
RMAQLNVVSE ADADAAKAKK LGLKVKNQPN GCLNSGAQFF CDYVVRWLMT DDALGATTQD
RKRLIFNGGL TIRTTIDMRY QRAAQQGVSG QVYKGDQAVG ALALIEPGTG NVKALAQSRP
MGTRKGETFL NYVVPKKYGD ANGAQAGSTF KAFVLAAAIS QGIPLTKTFP APNPGYFPEN
KFETCDGPYQ SSGVWEPKNS TSSSANPNLY EGTRNSVNTF FVNLELATGI CEPYKLAKQM
GIRSLTKDNI KPSFTLGVVD VSPLDMAEAY STFAARGLHC DARPVTQIAD AQGNVLKKYD
KQCTQVLASP VADAVSDVLR GVVEPGGFGS ALNPGQPAAG KTGTTNGNYS VWFAGYTPNL
AGAAMVAGVK PNGNQQTLDG KSIGGYVRAS TAGSTTAGPM WGDAFKAIAP LLPDENFVRP
SSTDVAGLLV TVPPVAGKTY DDARAELEAL GFTVARGGSV DSRLARGLIS YSSPGAGGQL
ATGDTVTLYP SDGSPAKPKG NGKGKKGKGK KGRGNG
//
