ID A0A0A2TKJ7_9BACI Unreviewed; 727 AA.
AC A0A0A2TKJ7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-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=N782_00755 {ECO:0000313|EMBL:KGP74606.1};
OS Pontibacillus yanchengensis Y32.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385514 {ECO:0000313|EMBL:KGP74606.1, ECO:0000313|Proteomes:UP000030147};
RN [1] {ECO:0000313|EMBL:KGP74606.1, ECO:0000313|Proteomes:UP000030147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y32 {ECO:0000313|EMBL:KGP74606.1,
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:KGP74606.1}.
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DR EMBL; AVBF01000001; KGP74606.1; -; Genomic_DNA.
DR RefSeq; WP_036815222.1; NZ_AVBF01000001.1.
DR AlphaFoldDB; A0A0A2TKJ7; -.
DR STRING; 1385514.N782_00755; -.
DR eggNOG; COG0768; Bacteria.
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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030147};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..302
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 352..697
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 704..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..727
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 727 AA; 82334 MW; 62BB600DF16373CE CRC64;
MRKKKNGKKS QVPFRLNVLF FIIFLLFSGL ILQLGVVQIL YGADAQEEIN KTTNQKVSVP
VPRGKMYDRY GNVVADTQPL YSITYTPMEK TPSQKRHLEL ARELAKLIDM NDEDTENIPV
RDQKDFWILN NEDAKKERLT EEELKYTDEE KAADEPTPYE ILLDKIDPEE DLDYGKKELE
IIAIKRKMDS AYAFTPHVIK NKNVTQEEYA RVAEHQQNLQ GINVSTDWKR AYPYEGHFRD
FLGSVTEDGL PKDSLDYFLA RNYSRNARVG ESGLEEKYEP LLKGQKKTIQ YETDRSGEIV
DENIINKGQQ GKNLQLTVDM ELQQKMDSIL QEHLTKARNK FPYENRFLDE AMAVAMDPQT
GEILGISGQT WNEDAEAFRN TGINAVTSPV APGSAVKGAT LLAGYDYGVV SAGEPIYDQP
IDLAGTPLKA SYSNLGYVND IEALKRSSNV YMFHIGMRIA GDPSYEKGEK LSYQPGRFQV
FRNYYAQFGL GVKTGIDLPS QTETAGLLSD NFRAGNMLDL AIGQYDTYSA LQLAQYVSTI
ANDGYRLQPR LVNDVREPIT NKDNKDQLGP IIQSNDTNVL NRISMDERYI QRVQTGFYQV
FNNQLGTADG YFADTEGYKA AGKTGTAQVN YYEPLRDENG KTYDYKRHEL ENLTLVGYAP
YEDPEIAFSV LVPNTGSISS PGYTQYQANK EIGRDILDAY FQLKEERGLN GDNGEEEGED
ESEETEE
//
