ID A0A0G1XAU6_9BACT Unreviewed; 640 AA.
AC A0A0G1XAU6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:KKW28413.1};
GN ORFNames=UY72_C0073G0002 {ECO:0000313|EMBL:KKW28413.1};
OS Candidatus Uhrbacteria bacterium GW2011_GWD2_52_7.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1618989 {ECO:0000313|EMBL:KKW28413.1, ECO:0000313|Proteomes:UP000034846};
RN [1] {ECO:0000313|EMBL:KKW28413.1, ECO:0000313|Proteomes:UP000034846}
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:KKW28413.1}.
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DR EMBL; LCRD01000073; KKW28413.1; -; Genomic_DNA.
DR PATRIC; fig|1618989.3.peg.905; -.
DR Proteomes; UP000034846; 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 65..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 106..281
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 321..620
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 640 AA; 69961 MW; B8AC04DB6F3B067B CRC64;
MWPWTHTKKP PSREVFNLRD DDHISLLRHA DADDVFDDIF SGRDLASEEV GTYVGNALSQ
GRRRLGFLIV FGAFSIFLGR IFLWQILDGQ EYRALADANR TSTVILPANR GVIKDRSGIV
LAWNEPSFQL IASPRELPSD VTEREALFTK AALTLEQTDT VSWIAALTVG KDDAAVLLAE
DIAYDRAISF IAQESMFPGL RMELGARRAY VTDAIPTLSH VLGYTGAIGD QEYEDVKQDG
YRRFDDIGKQ GIEKYYESEL RGTPGEEIRE VDAVGRAIRT LSRTETVDGT DLTLTLDARL
QAAIEYNLGK RLQTADVKRA SVIAMHPDTG EILALVSYPA YDANLFTDGI STTEYSALLN
DPNAPLFPRA TSGGYPSGST IKPVYAAAAL MEGVITPSTA FLSIGGMWVG PKFYPDWRAG
GHGLTNVYHA IADSVNTFFY IIGGGNESFN GMGLETXXSG IDLSNEASGF LPSKSWKLEE
KGEQWYIGDT YNVSIGQGDF LVSPLQIARS TAVFANGGNL VTPHLASGLS TEAVDIVPDD
VVTVIKDGMR QTITNGSGTM LNALPVEVAG KTGTAQWSSI ADPHSWFTGF APFDDPEIVI
TVIVEEGGDH ALALPVSYDI LNWWYENRQR ELEDTDSEHD
//
