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Database: UniProt
Entry: A0A0Q5B641_9MICO
LinkDB: A0A0Q5B641_9MICO
Original site: A0A0Q5B641_9MICO 
ID   A0A0Q5B641_9MICO        Unreviewed;       574 AA.
AC   A0A0Q5B641;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Penicillin-binding protein 2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASF46_09660 {ECO:0000313|EMBL:KQQ11490.1};
OS   Rathayibacter sp. Leaf296.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=1736327 {ECO:0000313|EMBL:KQQ11490.1, ECO:0000313|Proteomes:UP000050868};
RN   [1] {ECO:0000313|EMBL:KQQ11490.1, ECO:0000313|Proteomes:UP000050868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ11490.1,
RC   ECO:0000313|Proteomes:UP000050868};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ11490.1, ECO:0000313|Proteomes:UP000050868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ11490.1,
RC   ECO:0000313|Proteomes:UP000050868};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQQ11490.1}.
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DR   EMBL; LMNR01000001; KQQ11490.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q5B641; -.
DR   STRING; 1736327.ASF46_09660; -.
DR   Proteomes; UP000050868; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050868};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          39..189
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          246..551
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   574 AA;  60383 MW;  2F434C4BA1F9F72A CRC64;
     MIAAVVGLFI GKLVDIQIVR ANELTDAAAE SQSSSSVTYG TRGAIVDRAG AVLADTTTRY
     RLTTSPRNVA EFPREMPDGR EVVVSVEQAA AEIGAITGQS VEQVTGLVDA ELAENAKANY
     LVLAEGLDLE AFQKLVALDI PWLYFETQQG RTYPNGAVAG NLIGYVGADG AAQEGVEYTE
     NSCLAGRNGS ESFERSADYV RIPGSTVAET PAVDGGQVQL TIDSDLQYYA QQVLSQRVAE
     VGGSYGIVVV QEVETGKLLT VAETPTVDPN DVTASAAADR GSRAFQSPFE PGSTFKPMTA
     AMLIDQGLAT PTTHVVTPDT FEKNGVSFSD DFAHTPTNYT LTGILKDSSN VGIATIGSKL
     SAQQRYDYML KFGLDAPTAV GFPAESGGLL SDYQDWDGQT NYTTMFGQGV SATAIQVAGI
     YQTLGNDGVR LPAQLVAGCT TADGTVVDVP DATGTQVVSA GAAHDVVDML QTHYTDGWLA
     DYIHVDGYNI ATKTGTAQQP DGDGGYSSSY TVSLAGLAPA EDPKYVVTVT IADPVKMNTS
     QATAPVFQQV MTQVLKTNRV EPSTVPAVSY PTTW
//
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