ID A0A1M7AA97_9BACT Unreviewed; 613 AA.
AC A0A1M7AA97;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:SHL39566.1};
GN ORFNames=SAMN05720468_1265 {ECO:0000313|EMBL:SHL39566.1};
OS Fibrobacter sp. UWEL.
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=1896209 {ECO:0000313|EMBL:SHL39566.1, ECO:0000313|Proteomes:UP000184030};
RN [1] {ECO:0000313|EMBL:SHL39566.1, ECO:0000313|Proteomes:UP000184030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWEL {ECO:0000313|EMBL:SHL39566.1,
RC ECO:0000313|Proteomes:UP000184030};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; FRBE01000026; SHL39566.1; -; Genomic_DNA.
DR RefSeq; WP_073230743.1; NZ_FRBE01000026.1.
DR AlphaFoldDB; A0A1M7AA97; -.
DR STRING; 1896209.SAMN05720468_1265; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000184030; 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:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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 InterPro; IPR017790; Penicillin-binding_protein_2.
DR NCBIfam; TIGR03423; pbp2_mrdA; 1.
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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000184030};
KW Transferase {ECO:0000313|EMBL:SHL39566.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..238
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 277..604
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 613 AA; 68570 MW; 6DEAE04BDF0444B9 CRC64;
MRSSVNDNEI QQRKNWNVLV YLTGVALVFM VLLLRLFFVQ YVHYDENVQR SDNNRLRKVD
LIANRGFIYD RNGEVLVRNR PSYQIALQAT SLPRKKEARD SVFNRLLQIK DKSGERLFDS
LSLDTAFQRT RWIKNRPIRF FEDATPEQVA VVEEHSSELP GVVTLIESRR DYPYGTLASH
VLGYTSEISE EQLKLPEFQG YSQGDRIGQK GLEQYYDKEF RGKDGVKLVE VNASGREVGI
VDGVDGQDPV PGLHLVSTLD LKLQKVAEAA IPDSARGALV ALDPRTGEIL AMVSSPRLDP
NIFSLKRRER NKGWAHVALD SMRPLTNRAI SGTYPPASVF KLVTAGAGLE NGLLSEYKYY
PKACTGGYQY GSRYQKCWGT HGNLNVVHAL RLSCDVFFYQ AGLDIDMERI NEFGRRFGLG
EELLGVDIPG ERPGWLPDSI SFNKRNKRNG WRWARGLILN LSIGQGQIVT PLQQAVLVGS
LATNKGVYRP HFMKELRDEQ GNVVKRYEPE IIRSGRMKES THRVLMHAMD SVVNHPGGTG
KRGALPGIRV GAKTGSGEWK RGHKTHAWYA AVAPLENPEI AVAVIMEAAG GGGAVSAPIA
KKVLMEYFHI EAP
//
