ID A0A239PQ90_9PROT Unreviewed; 639 AA.
AC A0A239PQ90;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:SNT72459.1};
GN ORFNames=SAMN06297382_1504 {ECO:0000313|EMBL:SNT72459.1};
OS Amphiplicatus metriothermophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC Parvularculaceae; Amphiplicatus.
OX NCBI_TaxID=1519374 {ECO:0000313|EMBL:SNT72459.1, ECO:0000313|Proteomes:UP000198346};
RN [1] {ECO:0000313|EMBL:SNT72459.1, ECO:0000313|Proteomes:UP000198346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12710 {ECO:0000313|EMBL:SNT72459.1,
RC ECO:0000313|Proteomes:UP000198346};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; FZQA01000002; SNT72459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239PQ90; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000198346; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 Reference proteome {ECO:0000313|Proteomes:UP000198346};
KW Transferase {ECO:0000313|EMBL:SNT72459.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..237
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 272..614
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 620..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 71179 MW; 6B64D0B94C6CC22A CRC64;
MRINVHDPER QEILNRRAFL FGGAVSLGLV VVGGRLYQLQ ILDHDRYVEL AQDNQFNRRI
ITPLRGEIVD RFGKPLASNR KNFRVLFVPE QTRDVEGALD AISEIINISE EKRTRIMRQI
RRRAPFIPIE IENNLSWDQF SKINFQLPYL PGILPDVGET RDYPYGEAAA FVVGYVGAVT
ESDLSQAKSE EERILLRQPG FKVGREGLER TYDKELRGAA GSMNVKVNAY GRVIEELKDQ
AIPPVQGETL ALTIDADLQL AAMKELEGES AAAVVMDVVT GDILVLASTP AFDPNAFNIG
ISPQEWRALN ESPYKPLLNK PLSGVYPPGS TFKLVSAVAA QIAGYKPGFR AHCPGRLWYG
NRYFHCWKRE GHGWVDMKGS IKHSCDVFYY TIAKDIDVDI IADVAKKLGL GQTFELGIPG
QREGVVPSRE WKRRFFAGRP ENQPWFQGET LSVIIGQGYV TSTPLQLAVM TARIATGREV
RPRIVRVLGD IAAPPQPAAP LGIDPAYFDI VRVGMDAVTN EPGGTAYRSR LDNPDWRLAG
KTGTSQVYQI TAEERARGLT DPEDLPWERR DHALFVCYAP FDNPRYACAV VVEHGIGGAR
MAGPKAREIM RAVMTKDPAA RPAYDPRVVA QTPERSREG
//
