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Database: UniProt
Entry: A0A0L6JNZ4_9FIRM
LinkDB: A0A0L6JNZ4_9FIRM
Original site: A0A0L6JNZ4_9FIRM 
ID   A0A0L6JNZ4_9FIRM        Unreviewed;       715 AA.
AC   A0A0L6JNZ4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:KNY27087.1};
DE            EC=2.4.1.129 {ECO:0000313|EMBL:KNY27087.1};
GN   ORFNames=Bccel_2352 {ECO:0000313|EMBL:KNY27087.1};
OS   Pseudobacteroides cellulosolvens ATCC 35603 = DSM 2933.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Pseudobacteroides.
OX   NCBI_TaxID=398512 {ECO:0000313|EMBL:KNY27087.1, ECO:0000313|Proteomes:UP000036923};
RN   [1] {ECO:0000313|Proteomes:UP000036923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2933 {ECO:0000313|Proteomes:UP000036923};
RA   Dassa B., Utturkar S.M., Klingeman D.M., Hurt R.A., Keller M., Xu J.,
RA   Reddy Y.H.K., Borovok I., Grinberg I.R., Lamed R., Zhivin O., Bayer E.A.,
RA   Brown S.D.;
RT   "Near-Complete Genome Sequence of the Cellulolytic Bacterium Bacteroides
RT   (Pseudobacteroides) cellulosolvens ATCC 35603.";
RL   Submitted (JUL-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   -!- 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:KNY27087.1}.
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DR   EMBL; LGTC01000001; KNY27087.1; -; Genomic_DNA.
DR   RefSeq; WP_036941694.1; NZ_LGTC01000001.1.
DR   AlphaFoldDB; A0A0L6JNZ4; -.
DR   STRING; 398512.Bccel_2352; -.
DR   PATRIC; fig|398512.5.peg.2453; -.
DR   eggNOG; COG0768; Bacteria.
DR   OrthoDB; 9757901at2; -.
DR   Proteomes; UP000036923; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
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   Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 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   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000313|EMBL:KNY27087.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036923};
KW   Transferase {ECO:0000313|EMBL:KNY27087.1}.
FT   DOMAIN          52..298
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          348..690
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   715 AA;  80718 MW;  D227FD423C795992 CRC64;
     MKEFFKDRYN LLALFFILFG AVILVQLVNL QIINGKRYDE ESQRKLPNIR RVSAPRGNIE
     DRYGVPLAVN RVGYTIQIIK TKMNNDDRNE MLLKLVNIFE KNNDNYDKSL EKYLKIKPFA
     FGSAINGSSK KMESWKKDMD PNKKNVDLMS TPEGTYQFLR KKFDIDKKYS VEDAYKIMCI
     RYEMLIRGFT SLTALSLAKD VSRETVAELE ERHQEFPGIY TDVETFRKYT MGETAGHVIG
     FVRPMDEEEY EKLKEEGYRQ DEIVGKLGIE AFAEPYLRGK DGQKKIEVDI AGRLTEELET
     NPAIPGSTVK LTLDMNLQKV AMESIERNLE KIRSQADGKK NFGDAKTGSA VAMDVNTGEI
     LAMASYPSYD PSNFIAKPED KEAQKKIEEY YDVKKFELAK LSPTMNRVIN GRYAPGSTFK
     PLTAIAALET GVITKGYNTR YDPGYFDADG WMFKCLEYKH GHGNLTLKRA METSCNIYFE
     QVGCEAGIDN ISKWGTMFGL GKRTGIDLKD ESKGVLASRE YKKSDEFKRN YGRIEDWWKA
     DTAQASIGQI YNLVTPLQLV NYIGAIANGG KLMRPHLIKK VVKYDGSTVM ENKPDYTKIP
     VKKENLDLVI EGMKAVTMQE GGTAVSAFRN FPIEVAGKTG TAETGYEKTK SSNALFVCFA
     PADKPQIAIA VVVENGAWGA NTAPIAVDIM TEYFNLSGSA RSDDKLKTNQ IEFTR
//
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