ID A0A0G0J1M4_9BACT Unreviewed; 628 AA.
AC A0A0G0J1M4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Penicillin-binding protein 2, penicillin-binding protein 2 {ECO:0000313|EMBL:KKQ60877.1};
GN Name=mrdA {ECO:0000313|EMBL:KKQ60877.1};
GN ORFNames=US82_C0027G0018 {ECO:0000313|EMBL:KKQ60877.1};
OS Parcubacteria group bacterium GW2011_GWC1_38_22.
OC Bacteria.
OX NCBI_TaxID=1618897 {ECO:0000313|EMBL:KKQ60877.1, ECO:0000313|Proteomes:UP000034773};
RN [1] {ECO:0000313|EMBL:KKQ60877.1, ECO:0000313|Proteomes:UP000034773}
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:KKQ60877.1}.
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DR EMBL; LBUL01000027; KKQ60877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0J1M4; -.
DR STRING; 1618897.US82_C0027G0018; -.
DR PATRIC; fig|1618897.3.peg.773; -.
DR Proteomes; UP000034773; 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 43..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..255
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 296..620
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 628 AA; 68440 MW; 1EED5B45F9C83218 CRC64;
MLRNSNKFGR VSSGMEIEDY VLTATEKEAA RMEKPLEKKW FDILWYSMVI FVALLGMRVI
FLTVIKGSYY QGISKGNSIR NIVIKASRGR ILDRTGVALV NNVPSIDVVI IPADIPADES
SVAKVASELG KILGMDENEL KTILLSKKSK SLNPVLLKEN ISQDESLILL EKRINLPGIG
IEKTAIREYA DGPIFAHILG YEGKIEQKEM DANASYLLTD YIGKQGIEKS YEKYLRGVNG
ANQMEVDSMG NTKREVGIIN PKPGSDLIMS IDSELQKKLY DSMNAILEKT KTSTASAVAI
NPKNGEILAM VNAPSYDNNL FAKKISNADY NSLIQNPDKP LFNRAIAGEY PPGSTIKPVI
SVAALSEGVI NESTVIDGMG GILSLGSYSF RDWKAHGPSD VRTAIAESND IFFYTVGGGY
GNIQGLGMNR MKKWYELFGL GKLTGIDIGG EVDGLIPSEQ WKQEVVGERW SIGNSYHASI
GQGYVSATPL QLANMTAALA NGGTLYEPHL VSQIKKSNGE TTTLAPEIIQ SNFVSPEIMK
AVREGMRKTV LEGTATPLKD MPVEIAGKTG TAQFGVGAKQ EHGWLVSFAP YDDPQIAMAV
LVEGAGEGFT SALPITKEVY QWYFSGRE
//
