ID A0A2A2K3W9_9BILA Unreviewed; 356 AA.
AC A0A2A2K3W9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-terminal domain-containing protein {ECO:0000259|SMART:SM00936};
GN ORFNames=WR25_04188 {ECO:0000313|EMBL:PAV68628.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV68628.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV68628.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV68628.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
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:PAV68628.1}.
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DR EMBL; LIAE01009721; PAV68628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2K3W9; -.
DR STRING; 2018661.A0A2A2K3W9; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR InterPro; IPR012907; Peptidase_S11_C.
DR InterPro; IPR037167; Peptidase_S11_C_sf.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 1.
DR Pfam; PF07943; PBP5_C; 1.
DR Pfam; PF00768; Peptidase_S11; 2.
DR SMART; SM00936; PBP5_C; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..356
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012426217"
FT DOMAIN 250..340
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
SQ SEQUENCE 356 AA; 38154 MW; FE0AA10F46C0F410 CRC64;
MKPLIAAPFA IVALAMPSVA AAPQFQGIAP IAFMQDLSSG AVLYQRDADR RMPPASMAKM
MTVYVAFDMI KKGELKLDQM ITVRPETWAK WHGPQAGSTM FLSPNENVSV ENLLKGIRLG
LTNSHFGTAN GWPDNGVTYV TARDLAHLAT ATIQDFPDLY KRFYSLPNFT WGKTLGAGAD
ITQANRDPLL GRVAGADGLK TGHTEEAGYG FTGSAEQNGR RLVMVVAGLT SSKDRAEESV
RFMEWGFRAW QAKPVVAAGK QVSTAEVQMG SSSNVGLVAP RQLTVTLPAG AVPQMSAKVV
YEGPIKAPIT KGQHIADLVV TSPDLPEQRL PLVADKDVGQ AGFFGRAWAG LTSFFG
//
