ID A0A1H9WAG1_9BACI Unreviewed; 687 AA.
AC A0A1H9WAG1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN05518684_11570 {ECO:0000313|EMBL:SES30667.1};
OS Salipaludibacillus aurantiacus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=1601833 {ECO:0000313|EMBL:SES30667.1, ECO:0000313|Proteomes:UP000198571};
RN [1] {ECO:0000313|EMBL:SES30667.1, ECO:0000313|Proteomes:UP000198571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S9 {ECO:0000313|EMBL:SES30667.1,
RC ECO:0000313|Proteomes:UP000198571};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; FOGT01000015; SES30667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9WAG1; -.
DR STRING; 1601833.SAMN05518684_11570; -.
DR OrthoDB; 9766847at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000198571; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR007887; MecA_N.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627:SF25; PENICILLIN-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR Pfam; PF05223; MecA_N; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..687
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011778088"
FT DOMAIN 28..159
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 169..331
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 368..680
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 687 AA; 76770 MW; 44D0BCF9EDCE3314 CRC64;
MRHTTLFISL SALLLAGMTA CTGDEPENPE ETLEGYTEAW SEKAFSEMPD YLTENSRVEV
AGFEWDFEER YDAIYGELGI DTINISFESV DFEEEEIDLD ELEEIDYPVS VEMDTAAGVL
SYDTEIALTK FIPGNEEEEN EAEWGVEWDP SHFIKGMEEP EDTVSIETEQ PARGGIFDRN
GESLAVNGDI YQAGIVPERT EDLEETIEQF AEVLNLDEER VADLATRYPD NPDWNAPIQN
LSIDDDRLED LLEIPGVGAG KVEGRVYPHG ESTGHLIGHI GSITAEDLEE REGEGYGSTS
ELGKNGIELL MEEELRGSPG MTVSINREDG ELRETILETE PENGEDLYLT LDISIQDKMY
GVLNNDSGAG VVMDPKTGET LALVSVPTFN SNLRYLQLPD PRAEDMEDIN ILFERRFQGA
YSPGSVFKPL TAAAGLEEGT LDPEEELVIE GKQWQPDDSW GGYRVTRVND EETNVDLQTA
MMRSDNIYFA RQTLDMGQES FEEWAGKFGF GEPFPYDFPL YSSTLANEDI ENEILLADSG
YGQGEVQVTP VHMTALYTMF LNDGNLIYPL LFSDGLQNEN EGEMEELISP ENAEIVRESL
ISVVEDADGT AYRSDAGHNR ALAGKTGTAE LKEEQTAEDG EQIGWYVSFD YEEEDYLTTI
MVQNAEERGG SSYVVDLANE FWEKVEE
//
