ID A0A0G1APU5_9BACT Unreviewed; 656 AA.
AC A0A0G1APU5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:KKS27298.1};
GN ORFNames=UU84_C0007G0011 {ECO:0000313|EMBL:KKS27298.1};
OS Candidatus Yanofskybacteria bacterium GW2011_GWC2_41_9.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1619029 {ECO:0000313|EMBL:KKS27298.1, ECO:0000313|Proteomes:UP000033859};
RN [1] {ECO:0000313|EMBL:KKS27298.1, ECO:0000313|Proteomes:UP000033859}
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:KKS27298.1}.
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DR EMBL; LCCE01000007; KKS27298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1APU5; -.
DR Proteomes; UP000033859; 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 41..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..249
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 290..617
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 637..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 73256 MW; 00A6C2B20EF3A77A CRC64;
MFKRKKSYFI EVDREDRVTP EETLFDTGSN YSNLEKSIAD FYFKFIFGGI SVLSAVILIF
SFNISFFQHN YFQKIANQNK SASFSIASPR GVIFDRLGKP LAVNIPSFDL LVISKELRAM
PSGEMEESIN KMAGILKISP DDFKKFIDEQ IKDTAMFFAK SDLNKEMLLA VKNAEPTGFY
VISNMKRNYI DGRQFSHTIG YIGKVNENDL RDSHYYLTDL AGRMGIEAEY EDILRGEHGQ
LFFTRDGNES LNKESIPGKN LVLNIDSELQ KKLFNELYNI LAANNLFKAT AVIQNPQNGA
VLAMVSFPTF DNNSFIAGLT EKEQRNFLEG TNKPLFNRAI SGLYNPGSTI KPLMGLMVLE
EKIFSPQDTI KDCVSITIPN LFNRELSYVF KNWRQEYGLF NLRKAIANSC NIYFFTVGGG
FGNVPGLGIE KIAKYLSKSL ANMKLGIDLP GEEAGFVPTP EWKLKNKGEN WYQGDSYNVS
IGQGDLLVSP LWINSFVSAI ANGGTIYKPL MAQRILDQDK NTVKIFNSEK VSDLPFKPEI
IKEIKSDMEE TVISGTAKLL KDLPVRAGAK TGTAEVVKNK SINSLFTAFA PWENPEIAIT
VLVEGSASNQ GLAIQTANNV LKWYFGKDLK QKEAAISVPP SPAPNQLPTI TLAPSQ
//
