ID A0A1H9V0B1_9SPHN Unreviewed; 695 AA.
AC A0A1H9V0B1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:SES14717.1};
GN ORFNames=SAMN05518866_14514 {ECO:0000313|EMBL:SES14717.1};
OS Sphingobium sp. YR768.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1884365 {ECO:0000313|EMBL:SES14717.1, ECO:0000313|Proteomes:UP000199142};
RN [1] {ECO:0000313|Proteomes:UP000199142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR768 {ECO:0000313|Proteomes:UP000199142};
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}.
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DR EMBL; FOGE01000045; SES14717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9V0B1; -.
DR STRING; 1884365.SAMN05518866_14514; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000199142; 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 Reference proteome {ECO:0000313|Proteomes:UP000199142};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..239
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 271..585
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 642..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..695
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 74814 MW; 21E85BF868617029 CRC64;
MKFLTPKRKI VTEAAQSFTF SRRAMVVGGL QGAIGAVLIG RMAWISVVQN EKYSLLSESN
RVNMTLIPPR RGWILDRNGK PLANNRTDFR VDLIPQRVVD AEATITHLAQ LLKLEPDEVD
RIRDDLDKSA GFRPVQVADK LTYDQYAAIS VRLPDLPGVA PSQGFSRNYP AGATVGHLLG
YVGAATAEEF KARKDPLLIT PGFKIGKDGL EKAFDRHLTG KPGAKRVEVT ARGKIMQELT
TRQDTPGRSI KLTIDAGLQE YAGRRLATQS GSVVVIDCQN GDVLALASMP SFDPNSFSDG
ISHLEYEMLS KDDHVPLRNK TLQGLYPPGS TVKPMVALAL LEAGVGPQET VNCPGAIRVG
NTLFHCHKKR GHGPLNMRGA IAQSCDIYFY QMAQRIGMDR IASMAHRVGM GQKFDLPFPS
QSYGTVPDPA WKERKYNQKW QVYDTVNATI GQGYMLINPL QMAVMAARLA TGKQLMPNFI
HGAPRKEPAP VGSTEEHLVV IRDAMNAVVN GGGTGGAARS SIPGVMIAGK TGTAQVRRIT
MAERAGGVRG NAGLPFKLRD HALFQGFAPF DNPRYAIACI IEHGGHTIRN EDAPMIASDT
LSYLFDPAKA LEKLETLEKG WGGTPAERQA RQMAAFRLAK AIEKGEVPPP AENAAENATA
ANSAAPAPAP PAPPAPSADD EDVPPPPGAN GGATP
//
