ID A0A021VRW9_9CELL Unreviewed; 834 AA.
AC A0A021VRW9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Carboxypeptidase {ECO:0000313|EMBL:EYR63939.1};
GN ORFNames=N866_17075 {ECO:0000313|EMBL:EYR63939.1};
OS Actinotalea ferrariae CF5-4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Actinotalea.
OX NCBI_TaxID=948458 {ECO:0000313|EMBL:EYR63939.1, ECO:0000313|Proteomes:UP000019753};
RN [1] {ECO:0000313|EMBL:EYR63939.1, ECO:0000313|Proteomes:UP000019753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF5-4 {ECO:0000313|EMBL:EYR63939.1,
RC ECO:0000313|Proteomes:UP000019753};
RA Chen F., Li Y., Wang G.;
RT "Actinotalea ferrariae CF5-4.";
RL Submitted (JAN-2014) 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:EYR63939.1}.
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DR EMBL; AXCW01000059; EYR63939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A021VRW9; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000019753; 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.
DR PROSITE; PS51178; PASTA; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:EYR63939.1}; 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:UP000019753};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 728..794
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..819
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 87854 MW; 61A6D095F70FBF6F CRC64;
MVPTAPSSSA RPAGPGSSGP SGTAGPVRRG RRVNVFQAAA LLLAFLLTAG VGGVLAAGLV
MPAVATTSAI TDSSVELFEE LPTDLEPQRL SQQSRIWAAD GSLLATFFWQ NRIVVPLAEI
APVMQAAVIA VEDRRFYEHA GVDVEGMGRA LRTNLFSEDT EGGSTLTQQY VKNVLIDAAY
SRGDMQAVQD AMVSSGTAGV ARKLEEAKLA IALEKRMSKE QILEGYLNIA QFGPSVYGVE
SAARYYFSVS AKDLTYLQAA TIAGITQAPS ANDPVTQPER AQTRRNTVLL TMLQQEVITQ
EEYDAGVATP LVDTLAVSDP GNGCVVAGGA AYFCDYVTKV IAQSPEFGET QEERRELLLR
GGLDVYTTLD LRLQAIADEE VRAAVPVTDP SGLGHAISTI EPGTGKILAM AQNRVYNPRE
TTEPVAGETA VNYNADFAFG SSRGFQPGST FKPFVLAEWL RQGKSLNQVV DGELREYDSD
DFTASCDPNL YIDPGYRPTN FDGQGRGRMS VLQATANSIN TAYMNMVTQL DLCAMADTAE
AVGFHTAMGG ELLPVPSMVL GAQETSPMTM AASFATFAAG GVYCEPIAIT RVTDRDGNEL
PVPSANCRQA IDPGVAATVT YALQEVMTNG SGEGAQLSGR PSAGKTGTTN ENWHTWFAGY
TPQMSSAVWL GNPRGNVPQQ RIEINGRYYR AVFGSSISAP TWDRYMTRAH EGMPVQGFPE
PNSRLLFGEQ VTVPNVAGRS VQRAVDALAA AGFTARVSET PVDSPYPAGT VAYTDPAGGG
RSTVGSPVTI HVSSGRSAVP APAPAPAPAP APPAEPPPGQ GQGQGQGNGN GNGG
//
