ID   A0A1H8A4Q9_9FIRM        Unreviewed;       463 AA.
AC   A0A1H8A4Q9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase (Penicillin-binding protein 5/6) {ECO:0000313|EMBL:SEM65571.1};
GN   ORFNames=SAMN05216180_1109 {ECO:0000313|EMBL:SEM65571.1};
OS   Hydrogenoanaerobacterium saccharovorans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Hydrogenoanaerobacterium.
OX   NCBI_TaxID=474960 {ECO:0000313|EMBL:SEM65571.1, ECO:0000313|Proteomes:UP000199158};
RN   [1] {ECO:0000313|EMBL:SEM65571.1, ECO:0000313|Proteomes:UP000199158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.5070 {ECO:0000313|EMBL:SEM65571.1,
RC   ECO:0000313|Proteomes:UP000199158};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR   EMBL; FOCG01000001; SEM65571.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8A4Q9; -.
DR   STRING; 474960.SAMN05216180_1109; -.
DR   OrthoDB; 9791132at2; -.
DR   Proteomes; UP000199158; 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.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:SEM65571.1};
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   Protease {ECO:0000313|EMBL:SEM65571.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199158};
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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..463
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011588075"
FT   TRANSMEM        401..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..262
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   ACT_SITE        62
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        65
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   463 AA;  51838 MW;  4F32FB9F82F9D61B CRC64;
     MFKKMIALFI SAAIAASYTI TAFAAEASTP PPTVAEAYVV MDAETGQVLI EKNMNTKEYP
     ASITKILTVA LGLEKGKLED SVNVTQDAVF AIEPNSSHIA LQPDEIVTMK DLVYATMLPS
     ANDAANVIAE HIGGTMKDFA DMMNQKAEEL GAKNTHFVNA NGLPDDDHYT TAYDMALITK
     YAISVPGFMD VFGMKDTYTI YPTNKQPKER KFATEHMMLV ESKFYYEGTL GGKLGWTQEA
     KHTSVTLAEK NGMKLIVVVL KSDKYDKFKD SIALLDYSFD NFKRMSITKD KLKTFNISHY
     RSGGSAENVN IYGEKEYSFL VHKNMSDADV SIDYDVPEYY SDEKIHPAVV FETSSISMYE
     KIGSYPMDYQ ILALDAEADS TNADVPKKPT ITSQLIGILK VIGIVVLSVL GLVVLLFLVM
     LIIRGYNQFC KWHRRQKRIK RIQQYDDPDI ITRPLPPATR RKK
//