ID A0A1Y4VC04_9FIRM Unreviewed; 561 AA.
AC A0A1Y4VC04;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=B5E53_09515 {ECO:0000313|EMBL:OUQ67018.1};
OS Eubacterium sp. An11.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1965542 {ECO:0000313|EMBL:OUQ67018.1, ECO:0000313|Proteomes:UP000195664};
RN [1] {ECO:0000313|Proteomes:UP000195664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An11 {ECO:0000313|Proteomes:UP000195664};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUQ67018.1}.
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DR EMBL; NFLV01000010; OUQ67018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4VC04; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000195664; Unassembled WGS sequence.
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:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..561
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012034338"
FT TRANSMEM 479..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 100..333
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 34..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 191
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 561 AA; 60563 MW; 01573E0C530075CD CRC64;
MKRLFALIMA LSMSCYVCLP AQAQYSFQED TSMEAASEST TGSEKTAGDE VSSEAENTGR
AEEENTAASD VGGETGGEEG STDDNAEASA AAYGIEDLKG APDITADSAI LMDAASGAVL
YGKDENSKQY PASITKVMTA LLAIENCSMD DIVTFSNEAV NGIEPGSSSA GINVGAQLTV
RDTLYALMLV SANEAAAALA EHISGSDEAF ADLMNQRAAE LGCTGTHFTN PHGLPDEDHY
TTAHDMALIL QQAMKYQDFR TIAEAESYTL KKSDTLTDTL ELWNHSKIIR ENSDYYYKYA
EGSKPGYTMA AHNTLVTYAK KDGVELICVI LKDYGADNSY YDTTDLFEWG FDQVKALTPL
SSFDLNAALT ADSDIPADKI TNIQRLGCTF PSDYYILVKK DFDDSALTTS FVLDEDIHTG
RIGYINISAG DTVIGSAPVT YDLNSEAAQS YVSNGSADDN LETAPVDEGR MTPSKVFNYI
VRVIVVIIIL AIIISFIRRR QAEKRRQQRM LERKKKKASS NTRSGGTAGT GRSSSTSSSR
TRSGSSTSSG NKRNRRTGKR K
//
