ID A0A1I1GVX5_9ACTN Unreviewed; 797 AA.
AC A0A1I1GVX5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Membrane carboxypeptidase (Penicillin-binding protein) {ECO:0000313|EMBL:SFC15977.1};
GN ORFNames=SAMN04487968_10498 {ECO:0000313|EMBL:SFC15977.1};
OS Nocardioides terrae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=574651 {ECO:0000313|EMBL:SFC15977.1, ECO:0000313|Proteomes:UP000198832};
RN [1] {ECO:0000313|EMBL:SFC15977.1, ECO:0000313|Proteomes:UP000198832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7056 {ECO:0000313|EMBL:SFC15977.1,
RC ECO:0000313|Proteomes:UP000198832};
RA de Groot N.N.;
RL Submitted (OCT-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; FOLB01000004; SFC15977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1GVX5; -.
DR STRING; 574651.SAMN04487968_10498; -.
DR Proteomes; UP000198832; Unassembled WGS sequence.
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: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.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:SFC15977.1}; 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 Reference proteome {ECO:0000313|Proteomes:UP000198832};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 698..762
FT /note="PASTA"
FT /evidence="ECO:0000259|SMART:SM00740"
FT REGION 748..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 85076 MW; 7CB151EBEC5B423B CRC64;
MSSPRSDRLP AARLLPHLGV MLAVAAVLGV VVAGLAIPFA GVAGIGARNV ARSMDDLPAQ
LETGALSQRT RIVDSEGKLI TTLYDENRIN RPLSQISRNM TQALVSIEDY RFYQHGALDL
KGTLRAFVTN QANNGTVQGG SSITQQLVKM TLVAQAKASG DEDAIKAATE DSYARKIKEL
RYAIALEETH KKDWILERYL NAAYFGDGAY GVQAAAKHYF NVNANKLSLT QGATLAGLVK
NPTGYDPTNS PDRALARRNV VLDRMAQLHV ITEQQAADAK AAPLGLDVQP ARNGCVNSTA
PFFCDYVVNW LLKSGDLPGR TEKERMEYLQ SGGFTIKTTL DLRYQRAADD SVAAHVAPTD
QAIGALAMVE PGTGAVKALA QSRPMGRNKK KGQTYLNYVT PQEYGDSNGF QAGSTFKLFV
LASAIEYNGF PLHQKINSPH QKDIPQSNYK GCPGDGAQVG VWQVHNSTSD GMMDAYSGTR
ESVNTFFAQL EELTGLCNPY KLAKSMGVEL TNPTGPHGER VPSFTLGIAS VSPLEMAEAY
ATVAARGLHC DAEPVTAILD EHNKPVKEYG KSCQQVMAQG TADAVNDILR GVQEPGGFGG
DAGLGLSVPS AAKTGTIDSN MTVWYDGYTP TLATASMIAG ANSKGEWITL NGQSLKGGYV
ATAHGSTTAG PMWGDAMHVI QQWLPDQDFV KPDASVVSGV QVDVPFVGGM SVEHAKDVLR
EAGFRSSVGN RVYSGYSYGT VAYSNPSGKA AKGSPITLYP SAGPEPKRKH KKKRHGNSAR
LFDWPGNGNG NGPPFGH
//
