ID A0A3S0P9W5_9BACI Unreviewed; 723 AA.
AC A0A3S0P9W5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=EK386_03575 {ECO:0000313|EMBL:RUL55909.1};
OS Lysinibacillus antri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=2498145 {ECO:0000313|EMBL:RUL55909.1, ECO:0000313|Proteomes:UP000287910};
RN [1] {ECO:0000313|EMBL:RUL55909.1, ECO:0000313|Proteomes:UP000287910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SYSU K30002 {ECO:0000313|EMBL:RUL55909.1,
RC ECO:0000313|Proteomes:UP000287910};
RA Narsing Rao M.P., Zhang H., Dong Z.-Y., Niu X.-K., Zhang K., Fang B.-Z.,
RA Kang Y.-Q., Xiao M., Li W.-J.;
RT "Lysinibacillus antri sp. nov., isolated from a cave soil.";
RL Submitted (DEC-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUL55909.1}.
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DR EMBL; RYYR01000003; RUL55909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0P9W5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000287910; 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 CDD; cd06576; PASTA_Pbp2x-like_1; 1.
DR CDD; cd06575; PASTA_Pbp2x-like_2; 1.
DR Gene3D; 2.20.70.70; -; 1.
DR Gene3D; 3.30.70.2110; -; 1.
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; IPR005543; PASTA_dom.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 2.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 2.
DR PROSITE; PS51178; PASTA; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 584..644
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 723 AA; 79073 MW; DF7393B426017232 CRC64;
MLLLYGGLFF ALLIRIFYIQ ATGVVDGQKL EAKAAALYGK EAVLTAERGK ILDRNGNVIA
EDTLSYRLIA VVNPQATKNS KEPRHVVDPA ETAKVLAKHI PMEETEIYKI LTKKLSDGRQ
PYQVEFGVAG RSISHDKMEA IKKEKLSGIT FASDTKRYYP NGPFASHLIG FAQKENQDDG
TFQTIGKMGL ESIYNKELSG KNGTLKYESD IFGYLLPNSE KMVEPAENGD DIYLTLDKTI
QNFLEESMSK VYEQYNPESI VAVVANPKTG EILAMSQRPT FDPDTRVGLE NGWLNEVIEN
VIEPGSTLKT FTLATAIETG NWHPNATFQS GSYTILDRTI RDHNYVGWGK ISYLEGFQRS
ANTSMAYLLQ MIGDETFIDY LQKFGFGDKT GIDLPGEATG TLLATYPINR VTTSFGQGST
VTPIQLIQAM TAIANDGKMM QPYVINKIVD ANGKTVKQTE PTMKGEPISA ETAKQVRELL
ASTITSEVGT AKRFALEGYT VGGKTGTAQI ARPGGGYFSG KNNYLYSFLG LAPVEDPQLI
VYVAVKKPQL AVTEGGSEPV AAIFNTVVQN SLKYLNINPE NVAQVEKTSM GDYIGHNVES
AQVELTNQGL TPIVIGEGGT IIDQYPDNNL AITKGSLVFL KTDGVITLPS FDKWSLRNVL
VYKSMSGLPI ETVGEGYVES QSVSPNTIVV DSSPIVVKLK TPEEMYTEPL EETSAEGEIL
PQD
//
