ID A0A0G0QPT1_9BACT Unreviewed; 650 AA.
AC A0A0G0QPT1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:KKR03637.1};
GN ORFNames=UT31_C0014G0010 {ECO:0000313|EMBL:KKR03637.1};
OS Parcubacteria group bacterium GW2011_GWF2_39_13b.
OC Bacteria.
OX NCBI_TaxID=1618962 {ECO:0000313|EMBL:KKR03637.1, ECO:0000313|Proteomes:UP000034319};
RN [1] {ECO:0000313|EMBL:KKR03637.1, ECO:0000313|Proteomes:UP000034319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:KKR03637.1}.
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DR EMBL; LBWH01000014; KKR03637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0QPT1; -.
DR PATRIC; fig|1618962.3.peg.230; -.
DR Proteomes; UP000034319; 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: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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 59..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..273
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 314..644
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 650 AA; 72595 MW; 51FB81BCAD48AD1B CRC64;
MDFDQIFDKA PRKAFLPLKG FASLKLKTPW LSLEPEEIFL DAKKDQRQKI EEPIKKRNLF
LFYLLISFFL FVFIAEAGWL QIIKGPFYAI QAEKNRIRAV PIFAPRGIIY DQNGKQLVYN
VPVFNLVATP AYLPKNPEER ESNILKIAGI LEVDGNKMNE ILAKCDLFSF EPVILAENIS
REKILRWDAA GQNFPGINLE KNLRREYVDG FMFSHILGYV GRMDEKDNKK HKDYFLTETI
GKSGLEFQYQ DILRTLPGRQ ETEVNARGEI KKNGIISEST DVKSLILSIN AGLQNQLYGE
VSKILKKTNG TKAAAIAIDP RNGKILALVS FPGFNNNSLA EGITQEEYNK VFNNEDQPFF
NRVISGQYPP GSTIKPFFGA VALEEEVIRP NTVINDTGTI SIPNPYNPNI IYNFPDWKTH
GPVNIYSAIA QSCDIYFYTI GGGYGDFKGL GIDRLEKYLK LFGFGKITGV DLPNEKTGFV
PSANWKKEAK KEDWYIGDTY HLSIGQGDLT ATPLQIAVLT AAIANSGTVW QPRIVDKIID
SAKNIIKDIE PAGQKINFIS AENFGIIQEA MRETVLSGSA QYLKDLPIEV AGKTGTAQIS
AEASTNAWFT AFAPYKNPEI VLTILVEGGG EGSSAAVPIA KEALKWYFSK
//
