ID A0A1H6BPU6_9ACTN Unreviewed; 695 AA.
AC A0A1H6BPU6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:SEG62739.1};
GN ORFNames=SAMN04489712_107318 {ECO:0000313|EMBL:SEG62739.1};
OS Thermomonospora echinospora.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=1992 {ECO:0000313|EMBL:SEG62739.1, ECO:0000313|Proteomes:UP000236723};
RN [1] {ECO:0000313|Proteomes:UP000236723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43163 {ECO:0000313|Proteomes:UP000236723};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNVO01000007; SEG62739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6BPU6; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000236723; 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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000236723};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..239
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 285..659
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 673..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 74372 MW; D4DD79C4A07A2790 CRC64;
MNPKTHFRLL VLHVVVVTML LVLVGRLWNL QVVNGDHYRQ VAAQNRIRDI VVPAVRGLIL
DSSGRPLVRN RTALVVSVDR TVLSRQDDRG RAVLTRLAAT LGTSRADLEK RIRLCSPTVK
RPCWPGSPYQ PIPVDDRVDP KRALLIMERA EDYPGVIAQV QAVRDYPRPE GATAAQALGY
LQPITQEELD KRRGLRVTGY SGVDLIGRDG VEATYDADLR GEPGVRQVLV DSQGRVTGTA
REQAPVPGSS LVTSLDARVQ GAAEQAIKKA IDSARHSGAA ADAAAAVVMD VRTGRVVALA
SYPSYDPSIW IGGISQAEYD ALLGKSKGQP LISRATQGQF APGSTFKISS VAAAVADGYD
LHGTYPCPGS YNVGNRAFRN FEGQGHGDMN LHRALVVSCD TIFYKFAYEE WLRAGGTRPV
KKPKDPMVDM ARKFGFGSPT GIDLPSEAGG RIPDRRWKRE YWNATKSDNC KAAKTGYPEL
ARTNPSRAAY LKAVAAENCA EGFVWRAGDA ANFSVGQGDV LVTPLQLARA YAALANGGRL
VVPRVGLAVI RPDGTPVREI ASPPAQRLPV DDKVLAYMRK ALAEVPTQGT AAGAFSGFDF
KKVQVAGKTG TAEVYGKEDT SWFAAFAPAD KPRFAVVAMI SQAGTGASYA APAVREILEA
MYGLGGKPAA LKDGKLPDKL PKLRADGTVG AGAAP
//
