ID A0A1W2FHB8_9PSEU Unreviewed; 683 AA.
AC A0A1W2FHB8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase / D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:SMD21260.1};
GN ORFNames=SAMN05660733_06213 {ECO:0000313|EMBL:SMD21260.1};
OS Lentzea albidocapillata.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=40571 {ECO:0000313|EMBL:SMD21260.1, ECO:0000313|Proteomes:UP000192840};
RN [1] {ECO:0000313|Proteomes:UP000192840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44073 {ECO:0000313|Proteomes:UP000192840};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FWYC01000015; SMD21260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2FHB8; -.
DR STRING; 40571.SAMN05660733_06213; -.
DR eggNOG; COG2027; Bacteria.
DR OrthoDB; 56883at2; -.
DR Proteomes; UP000192840; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR NCBIfam; TIGR00666; PBP4; 1.
DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 2.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:SMD21260.1};
KW Hydrolase {ECO:0000313|EMBL:SMD21260.1};
KW Protease {ECO:0000313|EMBL:SMD21260.1}.
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 70404 MW; 807BA6A8F8156D34 CRC64;
MPDDPQWPTE DDDAESVAAA SQPTVQVNRP SVDQPTMRLP LAAVLSAPST QEPPRSSPIR
SAPNATGPGH ATLGVPTAGS GGSGRPSGDT AGGKSHGTIG PEVGQPRAVP MRVEPKKDQT
RVVPRPEQRT TELSVPPGKT ARVDQLPHLE QSWFDQQVKS DRQQHQPRPE QTKRVDQLQG
QAPLRQEPPR QEPPRAEPAR PVPPPPRQEP RDLPVTGYEE EPEDRLAEEP RKSRKPLFAV
LSLLVVAALA GATIYAVKEF GGTKAIETRP PAAPANVQPL VKAVTAGAPA PTAAGVKRAL
TGPAGNSALG TLTGSVIDPA SGTALWQQGD TTAATPASSL KILTAAAALL SLEKTDQLST
KVVQGAEPGT VVIVGGGDPT ISGAPGRSVY PGAATLDDLV GQVKAKGPVT KVQFDLSRYA
GEPLGPQWES VDIVGGSVAP IMPFMLDGGR IDQTNVNGTR TGSPAQAAAD AFAQRIGAPA
ATAGAAPAGA QVLGEIKSAP IEQLVDNMMQ ISDNVLTEAI AREIAIRTGN EPSFAGGVKA
VRDVLTKNGF DLTGANFVDG SGLSATNKIP PKLLTDVLTT AAKPTLDDAR TAKLRPLLTA
LPVAGGSGTL AGRYNGTAAP GKGWVRAKTG TLTGVNALAG MVVDVDGRVL VFSFMSASNR
NPETEVRPAL DVLAAALRGC GCS
//
