ID A0A1H0ZB67_9BACI Unreviewed; 673 AA.
AC A0A1H0ZB67;
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=SAMN05216231_1129 {ECO:0000313|EMBL:SDQ24695.1};
OS Virgibacillus salinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=553311 {ECO:0000313|EMBL:SDQ24695.1, ECO:0000313|Proteomes:UP000199444};
RN [1] {ECO:0000313|EMBL:SDQ24695.1, ECO:0000313|Proteomes:UP000199444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10449 {ECO:0000313|EMBL:SDQ24695.1,
RC ECO:0000313|Proteomes:UP000199444};
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; FNKD01000001; SDQ24695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0ZB67; -.
DR STRING; 553311.SAMN05216231_1129; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199444; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199444};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..673
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038509082"
FT DOMAIN 25..148
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 157..318
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 357..658
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 673 AA; 74013 MW; 01BD2FDFB5861340 CRC64;
MKKIIALIPI VLLVLVAACS NDEVTPQDRF DQYVKHWNEQ EFNEMYNMST TTSTEKYAKE
DYVERYKNIY EDLNIDNLNI TYDKLSEEKM ETAMEKGTAQ FPFTVEMETI AGPITFDYKA
TLIVEGEEEN ANWFVKWDPG FIFPAIKDGG EIGLSNIKPE RGEILDRNQL PLALNDTVHN
VGIVPGKLGS NPEKAKQKIS DLLGMSIESI NKNLDAGWVE PDLFVPLKKV PKSAEQTLNQ
LWEVSGVTER KVTGRVYPYG ESLGHLVGFT GPVTAEELEE MDSGAYSAND IIGKRGLELL
YEDKLRGEAG VEITVSKENE EDTILAEKPV KNGEDVVTTI DADLQMKIYE SYDGKAGTAA
AIHPKTGETL ALVSSPSFNS NEMGFGISQS RRDELQNNPK QPLLNRFTST YAPGSTFKPV
TAAIGLNNES IIPGEGIEIN GLTWSNGEGW GNYQVRRVSE SNGPVDVTNA LVRSDNIYFA
KKAVEMGSEK YVNGLQQFGF AKDFPFEYPI ETSTISSNGK LNDEVLLADT SYGQGEIQMS
ALHLAMAYTP FLNKGNLLKP TILADAEKSQ VWQEKLITGE QATLIQEALR NVVAAPNGTA
KGAHIDDLAI SGKTGTAELK KSGEESGPEN GWFVGYPTKN QDILISMMIE NTEKQGGSAF
TVGKVTELLK AVK
//
