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Database: UniProt
Entry: A0A1I0X4U8_9BACL
LinkDB: A0A1I0X4U8_9BACL
Original site: A0A1I0X4U8_9BACL 
ID   A0A1I0X4U8_9BACL        Unreviewed;       674 AA.
AC   A0A1I0X4U8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:SFA95687.1};
GN   ORFNames=SAMN05216312_102495 {ECO:0000313|EMBL:SFA95687.1};
OS   Cohnella sp. OV330.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=1855288 {ECO:0000313|EMBL:SFA95687.1, ECO:0000313|Proteomes:UP000198686};
RN   [1] {ECO:0000313|EMBL:SFA95687.1, ECO:0000313|Proteomes:UP000198686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV330 {ECO:0000313|EMBL:SFA95687.1,
RC   ECO:0000313|Proteomes:UP000198686};
RA   de Groot N.N.;
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}.
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DR   EMBL; FOKE01000002; SFA95687.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0X4U8; -.
DR   Proteomes; UP000198686; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; 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   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:UP000198686};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          67..258
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          311..649
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   674 AA;  74692 MW;  21BB8F003715EEB8 CRC64;
     MSDKLTEEAE RRGIRNRRHF SIRLNFFFFT VFGLFSVLII RLAYLQFVEG PNLKEQEHQL
     ATKDVSIPPI RGNIYDSTGF PIAYSTSTQS LYFTLEPGTK KAEGLALAAR IEAVFKQYGD
     QAKEPLTAAE IYEDMDFEGK VHYPFQQRRI KSGLTDQEIA YFSEHRDQFE GIDIVEESIR
     QYSTERVATQ LVGYMKQLSG ATSLDFYKDI NKDQEDPTLK YLDTEDVGFD GLELMYQSEL
     RGRNGLKTYP VNNQSQIIGP MELTKPVKGD NLYLTINKDV QLATQNAITQ HLQKIRTSNN
     KQERAPNAKT GYAVAMEVKT GKVVAMASMP DYDANVWQGG ISAKNYEQFQ FYLSNGAIRE
     VQAPYEDEKE RKKHPSSLVN LGSTQKPLTI LLGLNEGLIS TGSTMSDPGY FEFGREGHKT
     KVRNAGSAAN GTLTPSSAIA HSSNAYMAKM VGNSLYMRDG SKGLDVWDKY MKEFGLGVKT
     ESGLPGESKG SINYYIESKR GSAQSALIYS SFGQQGRYTA LQLAQYATTL ASRGTRLKPQ
     FVDRIEDTDG NVVQGYESEV LNKIEFPKSY WQTIESGMSQ VKVQGFDDFK YSFRRKTGTS
     EQDVGGGRVE NAVFIAYAPA NDPKLAVAVV VPEGGYGGWG AAPIARKIFD AYDAAVGLTD
     AGPAKTTTGT AAGQ
//
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