ID U5L7F3_9BACI Unreviewed; 638 AA.
AC U5L7F3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=N288_09165 {ECO:0000313|EMBL:AGX03754.1};
OS Bacillus infantis NRRL B-14911.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1367477 {ECO:0000313|EMBL:AGX03754.1, ECO:0000313|Proteomes:UP000017805};
RN [1] {ECO:0000313|EMBL:AGX03754.1, ECO:0000313|Proteomes:UP000017805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-14911 {ECO:0000313|EMBL:AGX03754.1,
RC ECO:0000313|Proteomes:UP000017805};
RA Massilamany C., Smith T.P.L., Loy J.D., Barletta R., Reddy J.;
RT "Complete genome sequence of Bacillus infantis NRRL B-14911 that has
RT potential to induce cardiac disease by antigenic mimicry.";
RL Submitted (JUL-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}.
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DR EMBL; CP006643; AGX03754.1; -; Genomic_DNA.
DR RefSeq; WP_022543694.1; NC_022524.1.
DR AlphaFoldDB; U5L7F3; -.
DR STRING; 1367477.N288_09165; -.
DR KEGG; bif:N288_09165; -.
DR PATRIC; fig|1367477.3.peg.1771; -.
DR HOGENOM; CLU_009289_6_0_9; -.
DR OrthoDB; 9804124at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000017805; Chromosome.
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; 3.30.450.330; -; 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:UP000017805};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 579..637
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 638 AA; 69612 MW; 253017C485AF66DF CRC64;
MRVSNVTVRK RLTIALLAGI LIFFIIDIRL GYVQFFLGSM LTDEAKELWS RDIPFEPERG
EIVDRNGVAL ATNVSAPTVY VVPRQVKDPD ETAEKLAAIL NMSEEKALQL ITKQASSVKI
PEGRKISHEK ATEIRAEGMA GVYIAEDSKR HYPFGNYLSH VLGFAGIDNQ GLMGLELYYD
KDLKGEKGSV KFYANAKGQR MNDMADDYKP PVDGMDLKLT IDSKVQTIVE RELDIAEAAY
NPDGIIAIAM NPNTGEILAM SSRPDFDPAN FRNVAPDIYN RNLPVWSSYE PGSTFKIITL
AAALEEGKVD LAEDHFHDPG YTEVGGAKLR CWKRGGHGSQ SFLEVVQNSC NPGFVELGER
LGKETLFKYI KDFGFGAKTG IDLQGESKGI LFDLENVGPV ELATTAFGQG VSVTPIQQVA
AISAAVNGGT LYTPFIAKEL IDPASGEIVM RKTPEAKRKV ISEETSKEIR LALESVVAQG
SGKKAFVDGY RVGGKTGTAQ KAENGRYLEN NHIVSFIGFA PADDPELVVY VAVDNPKGTI
QFGGVVAAPI VGNIMGDSLR AMGVEPRKEQ LEKELTWLDT PMVEVPDLVG ITKKELGELI
VNLKIDGSGE GETVVRQTPQ PGVKLKEGST IRLYFDDK
//