ID W5T9Y1_9NOCA Unreviewed; 434 AA.
AC W5T9Y1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Putative D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:AHH15914.1};
GN ORFNames=NONO_c11070 {ECO:0000313|EMBL:AHH15914.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH15914.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH15914.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH15914.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(2014).
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; CP006850; AHH15914.1; -; Genomic_DNA.
DR RefSeq; WP_025347433.1; NZ_CP006850.1.
DR AlphaFoldDB; W5T9Y1; -.
DR STRING; 1415166.NONO_c11070; -.
DR KEGG; nno:NONO_c11070; -.
DR PATRIC; fig|1415166.3.peg.1122; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_3_0_11; -.
DR OrthoDB; 3663940at2; -.
DR Proteomes; UP000019150; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF33; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB1; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:AHH15914.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:AHH15914.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019150};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..434
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039440610"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 107..338
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 39..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..78
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 194
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 434 AA; 44892 MW; D2196F5DEFD9D975 CRC64;
MNTRTSPHRR SRSLAAAVLA AGLLGVTTVA GLGTAAAAPA TTSTPFTTPN TDSCPNKTLP
PPPIDTSEVP APGETTPAPL PIPQQPVGGD KLGACGVVVP KGAPPLPADI SATAWVVADL
DTGKVLAAKD PHGRYRPAST IKTLLAAVAL PALDPHQVVT GTQDDANADG TRVGIGPGGR
YTNDQLFHAL LMCSGNDAAH AIAAQLGGDA ATVAKMNAMA KQLRAMDTRA ATPSGLDGPG
MSTSAYDLAT IFRHDMQNPV FADIIHTEQF DFPGYPADPK IPDDKDHPGF PIANDNRLLY
DYDGDLGGKT GYTDDARQTF VTGAERGGHR LVVTLLKADV LPIRPPEQAA RLLDYAFALP
AGANVGSLPN PNDKQDNTNV ALASPPVHEE PSAAGPVASH NSSNLRTVGI IGGMVLVIGL
GLFGWSRSGR SRRR
//
