ID A0A327Z0K3_9ACTN Unreviewed; 808 AA.
AC A0A327Z0K3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Membrane peptidoglycan carboxypeptidase {ECO:0000313|EMBL:RAK26024.1};
GN ORFNames=B0I29_12960 {ECO:0000313|EMBL:RAK26024.1};
OS Actinoplanes lutulentus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1287878 {ECO:0000313|EMBL:RAK26024.1, ECO:0000313|Proteomes:UP000249341};
RN [1] {ECO:0000313|EMBL:RAK26024.1, ECO:0000313|Proteomes:UP000249341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7090 {ECO:0000313|EMBL:RAK26024.1,
RC ECO:0000313|Proteomes:UP000249341};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-2018) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RAK26024.1}.
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DR EMBL; QLMJ01000029; RAK26024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327Z0K3; -.
DR OrthoDB; 3397599at2; -.
DR Proteomes; UP000249341; 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 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:RAK26024.1}; 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:UP000249341};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 77..260
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 427..655
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 725..782
FT /note="PASTA"
FT /evidence="ECO:0000259|Pfam:PF03793"
FT REGION 390..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..808
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 88113 MW; 8DBB3AE40984B8AA CRC64;
MGSWIRRRDH NIFVNAFVFL LCGLITGLVV AAAVFPFAAM SGLTLRAGEE AFASLPSELK
AFKSPQISRV YAADNKTQLT QFYDEFRSDV PLKGMSKFMR DAMVAAEDRE FFKHNGVDLK
GVARALVNNN QGGAKQGAST ITMQWVRMSL AYSATSPNDV LDATKDTPKR KVTEIRYAME
LEKQLTKDQI LERYLNIVPF GKQTYGIFAA SRVYFNKAPK DLTLGEAAML AGIVRAPSGY
DPTTSDGYAE IKQRRDNYVI PGMVELGFIT QAQADKAIKE PIPRKVRPVS NGCVSVAKNN
WGFFCDYFYR WWMDREEFGA TPYDRARRLK SGGYRITTTL DVKAQKNARD RIADLISEGN
KNALLLAAVQ PGTGKVRLLA ANRKFKLDDP ADPKNKISSD PAKARKGIRG SYPNTTNPLL
SGGGDITGYQ AGSVMKIFTL VAALEKKLPL AYTIKAEKRY ESKYIINRSN PSACPGTHFW
CPSNSGGGGE GIYNMWTGFG RSINTYFVPL EERVGAENVV GVAKRFGIQF RAAKDAEFAS
PGYSHQWGAF TLGVSATTPL DMANAYATLA ADGKYCPPTP IEQIVTRDGD KLDVGRSLCT
QATSPDVARA AVDAARCPVG DSALLGNCGG STAPDTRWVV GHPVFGKTGT TDKDKTASLV
AGTTSLVVAG YLVNPDYQNH KDRLQHAQVN PAVYRTLGDY MDGKPRVQFK RPENRKIAYG
ERRYIPDVEC DPLSRARNRL ERAGFSVDIG REVDSKCPEG TAAGTDPSGR TVKNGAVTIE
VSNGKSDEPE VPVPPGTPPS SAPPNPPR
//
