ID A0A1H0ITH9_9BACI Unreviewed; 444 AA.
AC A0A1H0ITH9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05518871_11718 {ECO:0000313|EMBL:SDO34520.1};
OS Psychrobacillus sp. OK028.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX NCBI_TaxID=1884359 {ECO:0000313|EMBL:SDO34520.1, ECO:0000313|Proteomes:UP000198927};
RN [1] {ECO:0000313|Proteomes:UP000198927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK028 {ECO:0000313|Proteomes:UP000198927};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
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}.
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DR EMBL; FNHY01000017; SDO34520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0ITH9; -.
DR STRING; 1884359.SAMN05518871_11718; -.
DR OrthoDB; 9791132at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000198927; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR012907; Peptidase_S11_C.
DR InterPro; IPR037167; Peptidase_S11_C_sf.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF11; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACA; 1.
DR Pfam; PF07943; PBP5_C; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SMART; SM00936; PBP5_C; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:SDO34520.1}; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..444
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011736271"
FT DOMAIN 312..414
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 67
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 131
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 444 AA; 49112 MW; 6447B2294A54CF96 CRC64;
MKKVWMTSMI KWLVLPMFLV SVVSTMPAAA KAEESLNLNV DAAILIDADT GKILYEKNSE
ASLGIASMTK MMTEYLLFEA IEEGKVTWDQ QYNVNEYTYK ISQDRRLSNV PLREDGSYSI
KELYEAMAIY SANAATIAIA ETIAGTEDNF IKLMNEKAAE MGLEGYKFVN SSGLNNGDLQ
GMHPASTNAA DENIMPAKSV AILAYNLMKD YPEVLETTKI PKKTFRAGTS DAIEMSNWNW
MLPGLVYEYE GVDGLKTGTT EFAGHSFTAT AEKNGMRVIS VVMKAVGADG KGSYKARFDA
TRALLDYGFS QFSKEEIVPA GYKIPEHKTL KVEKGKEDTV AIAVKDPISM VIRTNEKELY
KPVFTPSKET LEAEIKKDTV VGKVHLEKSE GTDYGYITDQ AAETDVVTIE AVERASWISL
MFQGIGKFFG NLWNSTTDFI GGLF
//