ID K2EFR4_9BACT Unreviewed; 600 AA.
AC K2EFR4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Penicillin-binding protein 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACD_16C00235G0019 {ECO:0000313|EMBL:EKE08923.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE08923.1};
RN [1] {ECO:0000313|EMBL:EKE08923.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKE08923.1}.
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DR EMBL; AMFJ01006130; EKE08923.1; -; Genomic_DNA.
DR AlphaFoldDB; K2EFR4; -.
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}.
FT DOMAIN 57..226
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 260..586
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 600 AA; 66238 MW; 51BD56F46AD8B77F CRC64;
MSRAETSKFF SRALFLGGFQ ICLVLLLFSR MVYLQIIEGS YYRVLADGNR IVTRPLVPLR
GRVYDKNGIL LVENETNFKL LLLADKKKDI EVALASLEAV ISLSPEAKEE ILKKAQKRQG
VESLVIKDNL TWDEVSAIEL HAMDLPGMTI EIGSKRRYPF AAEGAHLLGY VSSPSEKEEE
EDPSLGIPGL KIGKSGFEKY LNQRLKGTPG YSALEVNARR KIVRELNQIE SIPGEDICLT
IDERLQRYAY EVLSEHESAA AVVLDIQTGN ILALVSFPSF DPNLFTLGIN RNDWKDLQNN
PYVPLTNKAI SGLYPPGSTV KIFVALAALE AGIIDKTTSV QCPGYYYVGD HPFHCYKKEG
HGTVNVLRAI SESCDVFFYE IAKRVGIDRL STYYKNLGLG EGGIEGFPHS RKGLVPTKVW
KREKKKEKWT LSDTILTGIG QGYISATPME LAIAIARIAG GGKKVVPQLE KGTAHPFPDL
GFNPDHLDLV KEAMAHTANS PSGTAYPGRI LVEGKEMGGK TGTSQVRRIT LSQRRAGQTK
TTNLPWEYRE HGLFIGYAPL ENPRYAIAVI IEHAGGARSA VIAARDILLK AQALEEEPPL
//
