ID A0A0V8HF41_9BACI Unreviewed; 666 AA.
AC A0A0V8HF41;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=GA0061094_3138 {ECO:0000313|EMBL:SCC21465.1};
OS [Bacillus] enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=1402860 {ECO:0000313|EMBL:SCC21465.1, ECO:0000313|Proteomes:UP000181997};
RN [1] {ECO:0000313|EMBL:SCC21465.1, ECO:0000313|Proteomes:UP000181997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGD-1123 {ECO:0000313|EMBL:SCC21465.1,
RC ECO:0000313|Proteomes:UP000181997};
RA Seilhamer J.J.;
RL Submitted (AUG-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; FMAU01000004; SCC21465.1; -; Genomic_DNA.
DR RefSeq; WP_058299165.1; NZ_KQ758485.1.
DR AlphaFoldDB; A0A0V8HF41; -.
DR OrthoDB; 9766847at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000181997; 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..666
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038553509"
FT DOMAIN 27..150
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 157..320
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 354..661
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 666 AA; 74483 MW; A837A59245E058E0 CRC64;
MLKKLFLLSL VAAAGMLIAG CQEKAQPDDR LKEYVDLWND KKFEKMYDTY LSSSAKETYK
KEDVVKRTND IYGDLAVKDL KVKFKKPKEE KEWDKEKEAE FPVTISMNTL AGEVSYEETV
TLKKQEKDDE ENWFVDWDPS FILPDMEEGD KVGIESIPAK RGEIYDRNEN PLAINGEAFQ
IGIVPGEFNE SDLKKLSSLL EMSPEAIQKE LDQSWVKPEY FVPIKKLPIS ERPLALDIIE
LSGLYSKRVE ARQYPYGEAT AHITGYLGKI NAEKLENLKD KGYTAQSLLG ISGAEEVYED
KLRGQSGQRI YLTKVNGEET PVAEQEVKDG ENISLTLDAE MQKKLYDQMK DEVGTAAAVD
PKTGEALALV SVPSYDPNEF ALGMAGDKYD KIYNDPDKPL RNRFYQTYSP GSAMKAITAS
VGLKSGKLDP NKTFDIKGKR WQKDKSWGGY QVVRVFANDS VVDLESGLKY SDNIYFARVG
LEMGAEAFIK GLKDFGFGEE IPMSYPIQES QISNDGKISK EIQLADSAFG QGEVLMSVVH
LASAYGGIIN DGTMMKPVLL KDEEQGVWKK DLLTPEQSKL MRTDLRKVVS EGIAGKAQVS
GKEIAGKTGT AEIKSEQGTK GKENGWFVSY DQKNPEFILA MMLEGVEDRG GSTHTVQVAQ
KFYSNY
//