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Database: UniProt
Entry: A0A087B3F8_9BIFI
LinkDB: A0A087B3F8_9BIFI
Original site: A0A087B3F8_9BIFI 
ID   A0A087B3F8_9BIFI        Unreviewed;       599 AA.
AC   A0A087B3F8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Peptidoglycan synthetase {ECO:0000313|EMBL:KFI65558.1};
DE            EC=2.4.1.129 {ECO:0000313|EMBL:KFI65558.1};
GN   ORFNames=BCUN_0051 {ECO:0000313|EMBL:KFI65558.1};
OS   Bifidobacterium cuniculi.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1688 {ECO:0000313|EMBL:KFI65558.1, ECO:0000313|Proteomes:UP000029067};
RN   [1] {ECO:0000313|EMBL:KFI65558.1, ECO:0000313|Proteomes:UP000029067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 10738 {ECO:0000313|EMBL:KFI65558.1,
RC   ECO:0000313|Proteomes:UP000029067};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KFI65558.1}.
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DR   EMBL; JGYV01000001; KFI65558.1; -; Genomic_DNA.
DR   RefSeq; WP_033514791.1; NZ_JGYV01000001.1.
DR   AlphaFoldDB; A0A087B3F8; -.
DR   STRING; 1688.BCUN_0051; -.
DR   eggNOG; COG0768; Bacteria.
DR   OrthoDB; 9789078at2; -.
DR   Proteomes; UP000029067; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
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; 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:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 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   Glycosyltransferase {ECO:0000313|EMBL:KFI65558.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029067};
KW   Transferase {ECO:0000313|EMBL:KFI65558.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          61..231
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          276..575
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   599 AA;  63401 MW;  7391E0D4E81AF494 CRC64;
     MHPIRAFRHL GATMRRGVVI GLVIAFVALV CLGQLVHIQI IDGPSTALAA TRSRTVKAVL
     SAKRGRITDV NGTVLAQSVE RYTIIGNPQA AQEFEPTTCT ARTQSICHQL DGKPLSTTGA
     AAVAQLVAPL LGMDVAELGG KLSGTGQYAV LKKDVTPEVK RKIADLNLGG IIYGELSNER
     VYSGGALMGA LLGGVNDEGV GVAGIEQMED DTLTGTDGYQ VYQQGNGGEE IPGTMTESQA
     AVDGSDVRLS IDRDVQWRVR QILLESQQKY KAGWAIAVVQ NTQTGEILAL ADTDDYEAGS
     DDAKLNVARS VNEVFEPGSI GKVFTMSGLV QEKQHAMGDK FTVPDTLTLD GQTYKDSFNH
     GAEHWTMAGI LEQSSNVGTI LASDRYTDEQ RHAYLTKFGI GQASGLGLPG ESQGVLAPSG
     SWDGRTRNTV LFGQGYSTNA LQLTNAIAVI ANGGVRKPQV LVKATVSADG KVQETKPGES
     TRVIDESVAK QILNGMESVS EHYASQGFAG VPGYRVASKS GTAEVVGADG KLSSLISDYT
     AIIPADNPRF VVTVVLKDPE GSYGGLTAGP VFAEIGKFLM QKYEVPNSSP RKDAIPVEW
//
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