ID A0A0A2TAY6_9BACI Unreviewed; 721 AA.
AC A0A0A2TAY6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=N782_08720 {ECO:0000313|EMBL:KGP72977.1};
OS Pontibacillus yanchengensis Y32.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385514 {ECO:0000313|EMBL:KGP72977.1, ECO:0000313|Proteomes:UP000030147};
RN [1] {ECO:0000313|EMBL:KGP72977.1, ECO:0000313|Proteomes:UP000030147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y32 {ECO:0000313|EMBL:KGP72977.1,
RC ECO:0000313|Proteomes:UP000030147};
RX PubMed=26561516; DOI=10.1186/s40793-015-0085-y;
RA Huang J., Qiao Z.X., Tang J.W., Wang G.;
RT "High quality draft genome sequence of the moderately halophilic bacterium
RT Pontibacillus yanchengensis Y32(T) and comparison among Pontibacillus
RT genomes.";
RL Stand. Genomic Sci. 10:93-93(2015).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:KGP72977.1}.
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DR EMBL; AVBF01000020; KGP72977.1; -; Genomic_DNA.
DR RefSeq; WP_036818774.1; NZ_AVBF01000020.1.
DR AlphaFoldDB; A0A0A2TAY6; -.
DR STRING; 1385514.N782_08720; -.
DR eggNOG; COG0768; Bacteria.
DR OrthoDB; 9770103at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000030147; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 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 Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
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:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000030147}.
FT DOMAIN 59..299
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 348..684
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 697..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 721 AA; 82043 MW; AD52003D35149991 CRC64;
MGNKHKKKKS HLPFRLNVLF FAIFLLFSGL VLQLGVVQIL YGADAQDEID KTTNQTTKVP
VPRGKMYDKY GNVVVDNEPM YSITYTPMKS PSQQLHLSIA KKLAGMIQMD TGDITVRDKK
DYWILTQESP YKDRLTKEEQ TYTDEEAQAE EPRPYELLLE RIDINKDLNF SDQEKEIIAI
KRELDRAYSL TPHVIKNEDV SQEEYAVVAE HLNELPGINV TTDWKRKYPY GDSLRDFLGS
ITTDGLPKDE LDYYLSRNYS RNDRVGSSGI EKRYEMVLKG QKKQIQYTTD RNGNLVNEKV
VQEGNRGQDL VLNVDMELQK LMDESIRKHL KAAKQKFPIE NKYMKEAMAV ALDPDTGEVM
AISGQTWDEE DKEFYDSGIR AVNAPVLPGS AVKGGTMLAG YDYGVINYGE QIYDNPIKLK
GTPSKSSYQN LGFVSDIEAL KKSSNVYMYH VGMRIGGDPS YQPNEKLTFY PERFQVFRNY
YSQFGLGVKT GLDIPSETEG SGQQSDNFLG GNIMDLAIGQ YDTYTTMQLA QYVSTIANDG
YRVQPQIVSE IREPTTERNQ LGPVVQSNNT NVLNRVTMDQ KYINRVQEGF REVFTNGGTA
HTYFEDTDYE AAGKTGTAQA SYWEPMRDGE GQVIEYKERK LENLTLVGYA PYDDPEIAFA
IVVPYTGIVN GQYQTNKKIG RDLLDGYFKL KQARKEKESV NDITEEKMQA NDTLTTTENE
N
//
