ID A0A2W0CSD6_9MICO Unreviewed; 589 AA.
AC A0A2W0CSD6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:PYY35784.1};
GN ORFNames=DEI89_05775 {ECO:0000313|EMBL:PYY35784.1};
OS Curtobacterium sp. MCBD17_030.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=2175649 {ECO:0000313|EMBL:PYY35784.1, ECO:0000313|Proteomes:UP000248059};
RN [1] {ECO:0000313|EMBL:PYY35784.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCBD17_030 {ECO:0000313|EMBL:PYY35784.1};
RA Chase A.B., Gomez-Lunar Z., Lopez A.E., Li J., Allison S.D., Martiny A.C.,
RA Martiny J.B.H.;
RT "Emergence of Soil Bacterial Ecotypes Along a Climate Gradient.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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:PYY35784.1}.
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DR EMBL; QKLI01000004; PYY35784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W0CSD6; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000248059; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR Gene3D; 3.30.450.330; -; 1.
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 PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..214
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 259..566
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 589 AA; 62448 MW; 0C3CF08415BB6BDC CRC64;
MTKTLRNRRL RYSVVMIAVI ALVAVFVVRL VDIQVVQADE LSKAAESKRS IPVTLYGTRG
TIVDRDGTAL AESVVRYNIT TSPRLVKAFD GKLGGTRVKE ISVDQALSAI AKASGGEVAT
MQANIAADPK SDFAYLVKGI DVAHYEAVRA LQVPWLYPEQ QAARSYPTGA ATGNVTGFMG
TDGAQAGLEL AYQKCLAGTN GSETYERGED GVQLPGSTVT QKRAKDGGTL VTTIDSDLQY
MASQDIADAA QQLRAESATA TVVNAKTGEV LAVADYPTVD PNDVDATKDP GAYGSRALTA
AYEPGSTIKA AIAAALIDKG LASPTTQAVV PYSRTFPWGG TIHDSEFHPT ENLTLTGILR
DSSNVGITEL GSKLTTQQRY DVMREFGLFE PEPAIDYPGQ PTMDYGASPQ WDKQTDINSM
FGQGISTTAM QVSSVYQTLA NQGVRIPLHM VKGCQTEDGT TIDAPDVQSK RVVSAAAATQ
TVDMLQSVVT GGTLVGMKPI SGYNIAAKTG TAEVADGAKG YGADRIISVA GMAPAEDPQY
VVTVTFTKPQ TTKWSSGAAP AFRTLMSQVL EKYRVAPSTT QARTYPSTW
//
