ID A0A1U7PJ66_9BACI Unreviewed; 725 AA.
AC A0A1U7PJ66;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05428946_0284 {ECO:0000313|EMBL:SIT67853.1};
OS Edaphobacillus lindanitolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Edaphobacillus.
OX NCBI_TaxID=550447 {ECO:0000313|EMBL:SIT67853.1, ECO:0000313|Proteomes:UP000187550};
RN [1] {ECO:0000313|EMBL:SIT67853.1, ECO:0000313|Proteomes:UP000187550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MNA4 {ECO:0000313|EMBL:SIT67853.1,
RC ECO:0000313|Proteomes:UP000187550};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTPL01000001; SIT67853.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7PJ66; -.
DR STRING; 550447.SAMN05428946_0284; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000187550; 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; 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; 2.
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 587..647
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 682..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 79350 MW; D55E548B98BFE4C1 CRC64;
MFCVYGGLFF LLFGRFLYIQ VTGEVEGRPL AAMAQAKYER ENVLSADRGR ILDRDGQPIA
EDTLSYNLVA ILSKKASDGV KDKTKMRHVT DREKTAKALS EHIDLSYEEI LELLNRQDNP
DVYQVEFGSA GRNLSHEKMN QIKALHLPGI QFVKDKKRFY PNGMFASHLI GFAQKETQKD
GTTKTVGQMG LEKTFDEILT GENGKMEYES DTWGFLLPGT EEKVTPAVDG SDIRLTLDKT
IQNFVEDAMN RVQKEYSPER MSVIVADPKT GEILAMSQRP SFNPETKEGL SSNWLNEAVQ
YTIEPGSTMK VFTLASAIEE GVWAPNDHFK SGSYTMHDTT IYDHKRAGWG YISFLEGFQR
SSNVSMAYLL ERMKDEAFIG HLRDFGFGEK TGIDLPGEAA GVLNDVGPVE RLTTSYGQGS
TVTPIQMVQA ATAIANGGTM MKPYVIEEIR DPNTDKVLRK GEPEEKGKPI SAETAKTVLD
VMESVVTSEK GTGKIFDLED YSVAGKTATA QIPNGKGGWL HGTNNLLYGF LGMAPADDPQ
LIVYVNVHRP KLPPGEYGAI PVSKIFKPVM ENSLKHLNIR PDEEKEAKEQ ITLSDFEGTA
ADTVIKDLEA KGIKPVVTGG GGEVTGQFPQ SGTSILPGGL VILKTEGESV LPDFTGWSKR
SVLAFASLSG LTIEVHGEGF AASQSASPGS SPGGGAPTVV KFEKPDRLHA TPEEPSDEEE
EYPLD
//
