ID A0A1W2ELJ2_9FIRM Unreviewed; 604 AA.
AC A0A1W2ELJ2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:SMD10534.1};
GN ORFNames=SAMN04488500_12631 {ECO:0000313|EMBL:SMD10534.1};
OS Sporomusa malonica.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=112901 {ECO:0000313|EMBL:SMD10534.1, ECO:0000313|Proteomes:UP000192738};
RN [1] {ECO:0000313|EMBL:SMD10534.1, ECO:0000313|Proteomes:UP000192738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5090 {ECO:0000313|EMBL:SMD10534.1,
RC ECO:0000313|Proteomes:UP000192738};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; FWXI01000026; SMD10534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2ELJ2; -.
DR STRING; 112901.SAMN04488500_12631; -.
DR OrthoDB; 9770103at2; -.
DR Proteomes; UP000192738; 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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000192738};
KW Transferase {ECO:0000313|EMBL:SMD10534.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..220
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 266..587
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 604 AA; 65598 MW; 734AB1EF63AD4869 CRC64;
MWDEKSRRIK ILAIIVVGIV SLLVLRLVWM QLFQGAQYKK IAEQNRIRQI TAQAPRGTIY
DKNGAIIVAN RPSFAVSIIP GEYSNPQEAT PLLAVITGVP VDEINKLLKG SEDYPYTPVR
IKRDVDATTV AKIEERQYYL PGVVIEAIPV RQYVYKELAA HILGFVGSIS EEEYVRRKKQ
GVHPNDLVGK DGLEREWEEA LRGTDGGRQL EVNAVGEDVR SLGERASTPG KGLVLTIDAN
LQKATEEALN VQVEASRKMG QPAKGGAVVA LDVKTGGVLV MASTPAFDPN IFAGGITSKD
WNQLITNSNH PLNNRALQNS YPPASVFKIV TAAAALEMNL TTPQEIFDDR GVYVLNGWSF
YGWETKGLGK LTIIDGLAWS SDPVFYELGR RLGADNLASY ALTFGFGEKT GIKLAGEEKG
IVPTADWKEA NYGESWYPGE TLIAAIGQGY YLVTPLQQAM LTMAVANGGI VYKPMLVDKV
LTPDGSLIEK LQPEVLRTIY LRPEVWDTVR QGMMAVTAKG TGAAVFKGFP KTVAGKSGSG
ETGRGTTHSW FACYAPAEAP EIAVAVLVEE GGEGSMAAAP VTRRVLEAYF SIQSKPLPPA
PRTD
//
