ID A0A060NSS5_9BURK Unreviewed; 398 AA.
AC A0A060NSS5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=SMCB_2147 {ECO:0000313|EMBL:BAO84375.1};
OS Serpentinimonas maccroryi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Serpentinimonas.
OX NCBI_TaxID=1458426 {ECO:0000313|EMBL:BAO84375.1, ECO:0000313|Proteomes:UP000066014};
RN [1] {ECO:0000313|EMBL:BAO84375.1, ECO:0000313|Proteomes:UP000066014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B1 {ECO:0000313|EMBL:BAO84375.1,
RC ECO:0000313|Proteomes:UP000066014};
RX PubMed=24845058; DOI=10.1038/ncomms4900;
RA Suzuki S., Kuenen J.G., Schipper K., van der Velde S., Ishii S., Wu A.,
RA Sorokin D.Y., Tenney A., Meng X.Y., Morrill P.L., Kamagata Y., Muyzer G.,
RA Nealson K.H.;
RT "Physiological and genomic features of highly alkaliphilic hydrogen-
RT utilizing Betaproteobacteria from a continental serpentinizing site.";
RL Nat. Commun. 5:3900-3900(2014).
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; AP014569; BAO84375.1; -; Genomic_DNA.
DR RefSeq; WP_052468505.1; NZ_AP014569.1.
DR AlphaFoldDB; A0A060NSS5; -.
DR STRING; 1458426.SMCB_2147; -.
DR KEGG; cbab:SMCB_2147; -.
DR HOGENOM; CLU_027070_8_1_4; -.
DR OrthoDB; 9795979at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000066014; Chromosome.
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:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 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:BAO84375.1}; 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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..398
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001584834"
FT DOMAIN 291..382
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 66
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 126
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 398 AA; 42840 MW; 34CD55CD4C1C0DEC CRC64;
MTLPLLNRVF LYVLLCVGWL LGAASPAWAS SPQPPEIAAR AFVLLDATSG QVLAEREADR
EVEPASLTKL MSAYLVFEAL RAGRIERTQT LTVSERAWRM PGSRLFAPQG AQVPVEALLK
GMIVLSANDA TVALAEGVAG SVERFVERMN QQAQALGLTR TRFVNPEGMS APGHRSTARD
LAQLAARLSR DFPEFMPYFA IQRYHYPGAP AVNVNNRNLL LLRDPTVDGM KTGHTEAAGY
GIVASAQRPF AALGPGDAGQ RRLIAVVLGA NSENARAAQS QTLLNWGYAA FEAVRLFAPG
QVVSQPPVWQ GRASTVPLGR PEGVVVTVPA GQAAGLRTEL LRPEPLLAPL LKDQPLGTLR
VRNARGDVVA EVPLFVLEAV PQAGLLGRFW GALRLWIQ
//
