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Database: UniProt
Entry: U5L7F3_9BACI
LinkDB: U5L7F3_9BACI
Original site: U5L7F3_9BACI 
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
//
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