ID R7ZGI5_LYSSH Unreviewed; 738 AA.
AC R7ZGI5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=H131_06853 {ECO:0000313|EMBL:EON73178.1};
OS Lysinibacillus sphaericus OT4b.31.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1285586 {ECO:0000313|EMBL:EON73178.1, ECO:0000313|Proteomes:UP000013911};
RN [1] {ECO:0000313|EMBL:EON73178.1, ECO:0000313|Proteomes:UP000013911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT4b.31 {ECO:0000313|EMBL:EON73178.1,
RC ECO:0000313|Proteomes:UP000013911};
RA Pena-Montenegro T.D., Dussan J.;
RT "Draft genome of the heavy metal tolerant bacterium Lysinibacillus
RT sphaericus strain OT4b.31.";
RL Submitted (APR-2013) 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:EON73178.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AQPX01000013; EON73178.1; -; Genomic_DNA.
DR RefSeq; WP_010858329.1; NZ_KB933398.1.
DR AlphaFoldDB; R7ZGI5; -.
DR PATRIC; fig|1285586.5.peg.1389; -.
DR eggNOG; COG0768; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_009289_6_1_9; -.
DR OrthoDB; 9804124at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000013911; 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 598..658
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 738 AA; 81280 MW; 2A0B5E5AF44DBDE3 CRC64;
MKKKKFRFQW GAFLLLIFYG GLFFLLFTRM VTLQATGEAE GQALAAKAAA KYGKESAITA
SRGKIYDRNG QTIAEDTLSY RLIAVVNESA SPNPEKPRHV VDAEKTAKVL AEYIPMDEQA
IYKQLTKLKP DGEKPYQVEF GSAGRGINHE VMSKLKDEKL PGILFVSDLK RYYPNGVFAS
HLIGFAIKED KEDGSVTTKG KMGLEYTYDK ELTGENGKVK YQTDAFSYLL PTSEKMVTPA
KDGDDIFLTI DKTIQSFLEE AMTQVEQEYN PESMTAVIAE SKTGKILAMS QRPTFNPDTR
DGKNMKWLNE VIEETIEPGS TMKTFTLASA IDTDTWPPNA EYMSGQYTLL DRTIRDHNKY
GWGKITYLEG FQRSSNTAMA HLLKVIGDDV FIEYLDRFGF GKKTGIDLPN EATGTILSQY
PIQRVTTTYG QGSTVTPIQL IQAMTAIAND GTMMQPYVID RIVDSSTGKT IQNHEPVEKG
QPVSAGTAKQ VREILASTLT SKYGTAKDFV LDEYQVAGKT GTAQIPKANG EYSWGANEFL
YSFLGMAPVD DPQLIMYVSV TKPKLKGELG SVPVSKIFKP VMQNSLKHLN INPQDVQHVN
HVNIQDYTGK DTKAVQVELA NDGLQPVIVG AGGKIIEQYP KGKQKLVNGS TVFLKTAGDT
TLPNFTNWSL RNVLVFKSMS GLQIEVVGEG FAASQSVSAG TVISDSAPIV VKLKTPAESF
VKDVEASSEG EVEQIEDE
//
