ID A0A101P924_9ACTN Unreviewed; 795 AA.
AC A0A101P924;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN ORFNames=AQI95_11435 {ECO:0000313|EMBL:KUN07158.1};
OS Streptomyces yokosukanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67386 {ECO:0000313|EMBL:KUN07158.1, ECO:0000313|Proteomes:UP000053127};
RN [1] {ECO:0000313|EMBL:KUN07158.1, ECO:0000313|Proteomes:UP000053127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40224 {ECO:0000313|EMBL:KUN07158.1,
RC ECO:0000313|Proteomes:UP000053127};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces yokosukanensis DSM 40224, type
RT strain for the species Streptomyces yokosukanensis.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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:KUN07158.1}.
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DR EMBL; LMWN01000013; KUN07158.1; -; Genomic_DNA.
DR RefSeq; WP_067121042.1; NZ_KQ948209.1.
DR AlphaFoldDB; A0A101P924; -.
DR STRING; 67386.AQI95_11435; -.
DR Proteomes; UP000053127; Unassembled WGS sequence.
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:UniProtKB-KW.
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; IPR012907; Peptidase_S11_C.
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; PF07943; PBP5_C; 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:KUN07158.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053127};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 468..659
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT DOMAIN 702..782
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07943"
FT REGION 1..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 475
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 478
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 542
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 642
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 795 AA; 82284 MW; 7E153E6F5A4D9C2A CRC64;
MAGESPDRSK QRESSPEVTS GSASPVPEAG DPRLAVAREK DSSPEGVDTS TKVLSIRDVK
TTAPKPEAEE TPAEDAALRE AVSAWVRSAD TTRPANNSDT PANAATGLEE ADEEQAEPQN
GTAEKNDADA ETTDTEAKTD AEPETDAEGE TAAATDAEPK AEASEAEAET EAETETPRTE
DEPEAKSAPE GEDAAQAEDA SETEGASEGK DAPEAEAGPK GEDSPKGEDE AADADGEDAP
QGPPAADDET RADGAGGGDT DAEDEAEAAK PAEAPQATAP RAAVDQPTAV FKAVKPKQVD
QPTTMLKLGG ASGTKTPKTP STPKSDSESD SERTSKFVAL KNDMAPAAKP DVTTPVPQVG
PERTTQQPLP PRPPLDLLAE LTNTPPPPET AVRTIVRRVK IWTPLVVLLA IVFVIVQAVR
PLPSPTLVLS GKDTYTFGGG RTSLPWPGEG QGWIDADGVG TVGNFGKQTP VAIGSVAKTM
TSYIILRDHP LKTGQEGPKI KIDPKAETEG GYDKDGESTL NTIKAGDSLT EKQALSAVMI
PSANNIARLL ARWDAGSEAA FVKKMNDAAK ELGMTHTKYT DPSGLKESTV STAEDQVKLG
RAVTKIPALV AITSAASWTD PSGHYWNNYN ELPYKMGAIG IKTGSTTAAG GNLLFASRKQ
VGGQTVTIVG AILGQHKPKI LDTANAVSRT ALTAAQDALT SAKVLKKGDV VGYVDDQLGG
HTPIVVTKDV VAVGWSGLKV KLSFTSGKVP HTAKAGTQVG TLTVGDGTAG AVKVPVALQK
NLAEPGFGAK LTRLG
//
