ID W9AA14_9BACI Unreviewed; 643 AA.
AC W9AA14;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 Name=spoVD {ECO:0000313|EMBL:CDO02328.1};
GN ORFNames=BN988_00786 {ECO:0000313|EMBL:CDO02328.1};
OS Oceanobacillus picturae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=171693 {ECO:0000313|EMBL:CDO02328.1, ECO:0000313|Proteomes:UP000028863};
RN [1] {ECO:0000313|EMBL:CDO02328.1, ECO:0000313|Proteomes:UP000028863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1 {ECO:0000313|EMBL:CDO02328.1,
RC ECO:0000313|Proteomes:UP000028863};
RA Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequencing of Oceanobacillus picturae strain S1 isolated from
RT human gut.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDO02328.1, ECO:0000313|Proteomes:UP000028863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1 {ECO:0000313|EMBL:CDO02328.1,
RC ECO:0000313|Proteomes:UP000028863};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) 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:CDO02328.1}.
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DR EMBL; CCAX010000001; CDO02328.1; -; Genomic_DNA.
DR RefSeq; WP_036573250.1; NZ_CCAX010000001.1.
DR AlphaFoldDB; W9AA14; -.
DR STRING; 171693.BN988_00786; -.
DR eggNOG; COG0768; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000028863; 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; cd06573; PASTA; 1.
DR Gene3D; 3.30.10.20; -; 1.
DR Gene3D; 3.30.450.330; -; 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 InterPro; IPR011927; SpoVD_pbp.
DR NCBIfam; TIGR02214; spoVD_pbp; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF19; STAGE V SPORULATION PROTEIN D; 1.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
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; 1.
DR PROSITE; PS51178; PASTA; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028863};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 582..640
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 643 AA; 70096 MW; B7B3EF6BF69CF19C CRC64;
MKRVSTVTVK KRIVTVFLFG LLIFSIIDIR LGYVQFIIGD KLVGQANDLW TRDIVFEPER
GQILDTDGEV LADNVTAPSI VAVPRQISDP EETAEKLAGV LDVSKDKVLA DITKNASSVN
LRPEGIKISE KQELAIRTLN MDGIYLAKDS KRHYPNGEDL SHVLGFAGID NQGLMGLELY
YDDKLKGEEG SLSFYSDAKG RRLDSLADVY TPPEDGLNLK TTINSKVQTI IERELDLAVS
KYSPDGALAI AVNPKTGGVL GMSSRPNFHP ENYQEVDSNI FDRNLPIWST YEPGSTFKII
TLAAALEEAV VDLEEDEFND DGSISVDGSE LHCWKSGGHG NQTYLEVVQN SCNPGFVTLG
QKLGEEKLFS YIDNFGFGEK TGIDLQGEGN GILFAEDQVG PVELATTAFG QGVSVTPIQQ
VMAVAASVNG GYLYEPYLAE SWIDPKTNKI VETHEPNVKR KVISEETSEE VRYALESVVA
QGTGRPAYVD GYRVGGKTGT AQKVGPDGNY MENNYVVSFI GFAPADDPEI VVYVAVDNPK
NTVQFGGVVA APIVGQIIGD SLQAMEVEPS AGGMDKEYLW PEEPKVEVPD LIGLTKEELA
EYMTNLSIET SGEGEYIIDQ APAPGTKVEQ GSKMRIYLSE KDR
//
