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Database: UniProt
Entry: A0A0V8HF41_9BACI
LinkDB: A0A0V8HF41_9BACI
Original site: A0A0V8HF41_9BACI 
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
//
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