ID D3R0L4_MAGIU Unreviewed; 748 AA.
AC D3R0L4;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 OrderedLocusNames=HMPREF0868_0383 {ECO:0000313|EMBL:ADC91054.1};
OS Mageeibacillus indolicus (strain UPII9-5) (Clostridiales genomosp. BVAB3
OS (strain UPII9-5)).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Mageeibacillus.
OX NCBI_TaxID=699246 {ECO:0000313|EMBL:ADC91054.1, ECO:0000313|Proteomes:UP000008234};
RN [1] {ECO:0000313|Proteomes:UP000008234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPII9-5 {ECO:0000313|Proteomes:UP000008234};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL Submitted (DEC-2009) 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; CP001850; ADC91054.1; -; Genomic_DNA.
DR RefSeq; WP_012993898.1; NC_013895.2.
DR AlphaFoldDB; D3R0L4; -.
DR STRING; 699246.HMPREF0868_0383; -.
DR KEGG; clo:HMPREF0868_0383; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_371646_0_0_9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008234; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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:ADC91054.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008234};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 407..496
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT REGION 44..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 532..574
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 51..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 81171 MW; 9B5C10401483475F CRC64;
MSIPFFHSTR RLGRSLIALA LSFSIGCGIG FNISAEEKSA KAEATELAEK SEHSQSQSTD
AASGHKTSEN KVSNSNPAAS QPTVSQPNGS QSTVTPAKEG KVAPPKEDPT IKRTSDGRLL
NWPTERGFTF NTNANEIKIK QNDLRSNKFA TYIFNNNGQI QSVFTKKEHE KFAPATMTKL
FSVLLAYDKL NQRLNEETDI IPSDVDGLAE VGARIIGFKV GESLPIADLF LGAVMESGAD
AIRALARLSY GDENDFVKAM NEKAKALGMN DSHFSNCTGL SADGDSTSVH DMAIVMALCA
TRPQLVQMLC TAGYTTQKTD FHPYGIALNS ILFNDIEQAK AQSEGRKVYI QGGRPGWSPD
GLFNLMTFAH VGKKLLVVVS AGADQAQARF ADHDNIYNQL IGAQHDVTVL TPHQPVGEIK
LINGRSDKVE LANGPDSFTA SLPVMLFAED VDIKLQVPER IDAPVKKGQE IGQIQVNLNG
RLLHTTPAIA AESYRARLVI GLASGITAFY QKVPYLFVLI LLVLIALTIF YIIRLNKKQA
LLEQRLREEA EARLAELERK RRLEEDERRW QELNKGRAYY STAQDPYRIE KHYETPLMEP
DEPVDNSVLL GEAGKVQLLD PATLLNDSDK NVKKINPSVG TAPTRLAGSA ASQAASRLAG
HAAGQAASLL ANQAANLTSR PAPTRLGVDT IGQAPAPTRL GGQTADRTAS NTNVKSSTPS
SPNPAPTTIH PVRIQPPEKS NPEQPQQK
//
