ID A0A1E5Q2D8_9ACTN Unreviewed; 970 AA.
AC A0A1E5Q2D8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=BGK67_14570 {ECO:0000313|EMBL:OEJ35712.1};
OS Streptomyces subrutilus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36818 {ECO:0000313|EMBL:OEJ35712.1, ECO:0000313|Proteomes:UP000095705};
RN [1] {ECO:0000313|EMBL:OEJ35712.1, ECO:0000313|Proteomes:UP000095705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-1-1 {ECO:0000313|EMBL:OEJ35712.1,
RC ECO:0000313|Proteomes:UP000095705};
RA Chen X.;
RT "The complete genome of Streptomyces subrutilus 10-1-1.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:OEJ35712.1}.
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DR EMBL; MEHK01000001; OEJ35712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5Q2D8; -.
DR STRING; 36818.BGK67_14570; -.
DR Proteomes; UP000095705; 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: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 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 Reference proteome {ECO:0000313|Proteomes:UP000095705};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 638..837
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 1..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..563
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 647
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 650
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 716
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 816
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 970 AA; 97596 MW; 323C9C0AD4D70162 CRC64;
MAGESPDKSV DEGTPGAAST SAESDPRLSV FRQRNPDPQA PADTAVDAEP DADGSGGRDP
LRDAVAAWVA TADEPTADPD ADADPEDGPV SRPTGSARPA PADPTPAPTG SASTQPAAPG
GASAPAGDQR TTAFRAVEPP APQPAEPDSA ATPARPPHGE AADAPTPGSA SAARPTGDAP
ADAPGAGSPA TPERPSRAES ADASRASTPA SGSASAEGGS AGDERAAASR AAGPASTSGA
GAAATPERSA PDEDAGASRA PGSDSASAGD QRTTAFRAVR PPASESAEPG SASAARPTGD
APADAPRATA APGAGSASAQ GGSAGDERGA ASGGDQRTAA FRAVKPGGPA AKADDSERTA
VFRAVRPAAS EAPPAGSASA DEPGGGERTA AFRADKPAVG GQPKGAPADE PGDSERTAVF
RAVKPAAGED APVKEPAPRE RTGVFRIPSA DAGDSERTAT FRAVKPPAPA DRPADSASAA
SPASPAPPAA APPKASTFVP LRTDEPGQEQ PKPKAAAPAA APAASTPASM DRTERTTQQP
LPPRPPLDML ADLTNNPPPP PSPLRTAVRR FKIYFPLVVL LAIILAVVQL VRPLPEPRLV
MTAKSSYTFG GAKPELPWPG EGQAYMAAAG LGTLGQSGEQ KPVPIASVTK SMTAYIILRD
HPIKKGEQGA MIDVDKTAET EGKKNDSVNN ESTLDTVKEG DKISEYDAIA ALMIPSANNI
ARLLARWDSG SQEAFVKKMN DTAKELGMAN TTYTDPSGLD ATTVSTAEDQ VKLGLKLVEI
ETLLDITRKP SWVDPSGKKW DNWNRLVPYN DSLGIKTGTT TKAGGNLLFA AQKKIGNTNQ
LIVGAVLGQH KPPIIDSVIS ASKQLMIGTQ KALEGAPVVK KGQVVGYVDD GLGGRTPVVA
TADVQAIGWA SLTVNVKLAD GGGKIPQTAK AGTEIGVLTV GEGASQVKVP VALQSELASP
GLGSKLTRVG
//
