ID A0A0W1QP55_9SPHN Unreviewed; 675 AA.
AC A0A0W1QP55;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:KTF70039.1};
GN ORFNames=ATB93_00820 {ECO:0000313|EMBL:KTF70039.1};
OS Sphingomonas sp. WG.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1592629 {ECO:0000313|EMBL:KTF70039.1, ECO:0000313|Proteomes:UP000052965};
RN [1] {ECO:0000313|EMBL:KTF70039.1, ECO:0000313|Proteomes:UP000052965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WG {ECO:0000313|EMBL:KTF70039.1,
RC ECO:0000313|Proteomes:UP000052965};
RA Li H., Feng Z., Sun Y., Jiao X., Zhou W., Zhu H.;
RT "Draft Genome Sequence of Sphingomonas sp. WG, a welan gum producing
RT strain.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KTF70039.1}.
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DR EMBL; LNOS01000020; KTF70039.1; -; Genomic_DNA.
DR RefSeq; WP_019368794.1; NZ_LNOS01000020.1.
DR AlphaFoldDB; A0A0W1QP55; -.
DR Proteomes; UP000052965; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000052965}.
FT DOMAIN 60..232
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 264..579
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 630..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 675 AA; 73036 MW; DA99B3F7A18CA876 CRC64;
MVRITEATQT YSFSRRAVVL GAAQGAVGMV LAGRMAWLSV FENERYQLLA ESNRVNMTLI
PPRRGWLLDR SGKPLASNRT DFRVDLIPDR IVDKDKLLAE LTQLLKLAPE DLARIETDLK
RAGGFRPVQV AENLDWDRFA AILVRQPELP GVAPTRGYAR HYPLGAGVGH LVGYVGTASA
EQYKQDKDPL LVTPGFKLGK DGLEKTLDKR LRGKPGAKRV EVTAHGRPVR ELETRADHPG
ESIKLTIDAG LQEYVARRLG TNSGSAIVID VASGDILAMA SMPSYDPNSF SDGISQTEWK
MLSEDDHVPL MNKVLQGLYP PGSTVKPMNG LALMAAGVSP SERVFCSGAM RVGSGVFHCH
KRGGHGPIDL KNAIMQSCDI YFYEMIRRVG YDAIAPMARM LGLGQKFDMP FTTQRYGTVP
DSAWKLKKYH RPWTVADSLN ASIGQGYVLA NPLQLAVMAS RLASGKILVP RLLARGPSGA
SPLPVSEEHL AIVREAMYGV VNGGGTGGAA RMYVPGVSIA AKTGTAQVRR ITMAERRTGV
LKNAALPFKM RDHALFVCFA PADNPKYAAG IVLEHNGHTV RNLDTPLIGR DIMTYLFDRD
QAMKTLAEVE PTWGGDYTTR MAAQADAFRQ AQNAPPPPAP EDAAEAASVV ASDAANATVN
TTTSNVAPTG SADRD
//
