ID F7S3R0_9PROT Unreviewed; 612 AA.
AC F7S3R0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:EGO96210.1};
GN ORFNames=APM_0961 {ECO:0000313|EMBL:EGO96210.1};
OS Acidiphilium sp. PM.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=1043206 {ECO:0000313|EMBL:EGO96210.1, ECO:0000313|Proteomes:UP000004823};
RN [1] {ECO:0000313|EMBL:EGO96210.1, ECO:0000313|Proteomes:UP000004823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM {ECO:0000313|EMBL:EGO96210.1,
RC ECO:0000313|Proteomes:UP000004823};
RX PubMed=21914891; DOI=10.1128/JB.05386-11;
RA San Martin-Uriz P., Gomez M.J., Arcas A., Bargiela R., Amils R.;
RT "Draft Genome Sequence of the Electricigen Acidiphilium sp. Strain PM (DSM
RT 24941).";
RL J. Bacteriol. 193:5585-5586(2011).
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:EGO96210.1}.
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DR EMBL; AFPR01000092; EGO96210.1; -; Genomic_DNA.
DR AlphaFoldDB; F7S3R0; -.
DR HOGENOM; CLU_009289_1_2_5; -.
DR Proteomes; UP000004823; 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};
KW Transferase {ECO:0000313|EMBL:EGO96210.1}.
FT DOMAIN 60..229
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 262..591
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 612 AA; 65922 MW; DA046FA35FEF483F CRC64;
MNAQRDKKQR AVFTRRAMII GGSQVALFSA LTARLYEMEI VDHSRYSRLA RKNAVSERLI
APERGLITDR NGVILAGNRQ QWQALFLMTA ASDPAATIAR LERIVSLSPA DRARLAKLAT
GPIHFLPILV KKDLGWDEMA RLEVHRPSLP GLIIDRGFRR FYPLGPLTAH PVGYVVRPDS
ADAGREPVLA LPGVRVGGSG IEKSANAALF GSPGIVEDEV DAGGAVVRVI TRRPAREGHA
VGLTLDAGLQ RTAAGALNGR PGAAVLIDTS TGDLLAMASA PSFDPTWFDD GVPDHVWRRW
TSKAAHHPLT DRATGGLYAP GSSFKPTVAL AALEAGAITG DTRFFCSGHM KIGNRIFYCW
LRSGHGSMDV ASALQQSCDI FFYHVAMRTG IDRMAAMARH LGLTGREALA LPNVAEGFIP
TRRWAKQRQI DWTKGDTAVQ GIGQGYTVLT PLALAVMAAR IGTGRAVRPR IIRTVGAVER
THPAATTLSL SDRHLALVRQ GMAEVVNTPL GTAWGARLAL RGARMAGKTG TAQVIGESAE
MEAENYNDAE LPWQDRPNAL FVGYAPLDRP RFAAAVVIEH GTLLGPVKIA RDLFAAALSR
RRLAYGDESR PA
//
