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
//