ID   A0A174TWK0_9BACE        Unreviewed;       653 AA.
AC   A0A174TWK0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:CUQ14664.1};
GN   Name=ponA {ECO:0000313|EMBL:CUQ14664.1};
GN   ORFNames=ERS852494_04094 {ECO:0000313|EMBL:CUQ14664.1};
OS   Bacteroides caccae.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=47678 {ECO:0000313|EMBL:CUQ14664.1, ECO:0000313|Proteomes:UP000095657};
RN   [1] {ECO:0000313|EMBL:CUQ14664.1, ECO:0000313|Proteomes:UP000095657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5834880 {ECO:0000313|EMBL:CUQ14664.1,
RC   ECO:0000313|Proteomes:UP000095657};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CZAI01000013; CUQ14664.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A174TWK0; -.
DR   STRING; 47678.ERS852494_04094; -.
DR   Proteomes; UP000095657; Unassembled WGS sequence.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR011812; Pep_trsgly.
DR   PANTHER; PTHR30400:SF0; BIOSYNTHETIC PEPTIDOGLYCAN TRANSGLYCOSYLASE; 1.
DR   PANTHER; PTHR30400; MONOFUNCTIONAL BIOSYNTHETIC PEPTIDOGLYCAN TRANSGLYCOSYLASE; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095657};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          436..587
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
SQ   SEQUENCE   653 AA;  74540 MW;  25384F7653801F98 CRC64;
     MMKTNSQKRI LPLALSGGIL ICLICIYSGR SVLLRSIVNR HTSRIEQTHG LCIHYDKLEM
     NGLNEISLQG LSVIPEQRDT LFTLASTRIK LNFWKLLTKK IEVSYIAAED IRLTFTKQDS
     IANYDFLFKK DRKVPSQTSG QTVTEINYAE RINKLLNLCY GFLPENGQLK QIYITERKDS
     NFVSMVFPSF IIKENKFRST IEIHEDTLTR HWIADGELKQ SANTLMAKLY SADSTKVSIP
     YITRRFGAKV TFDTLSYSMT KESNGKNQLY LNGKAKVNGL DIFHKVLSPE VIHLDRGHLG
     YQMNISDHSF ELDSTTTVIF NKIQVHPYLR AEKKKDLWHF TAAVDKSWFP ADELFSSLPK
     GLFNNLEGIK TSGELAYHFL LDIDFAQLDS LKLESELKER NFEIVEYGDT QLSKMSGEFV
     YTAYENGMPV RTFPVGPSWE HFTPLDSISP ILQMSVMQSE DGAFYYHHGF LPDALREALI
     YDLQVKRFAR GGSTITMQLV KNVFLNKNKN FARKLEEALI VWIIETKRLT SKERMYEVYL
     NIAEWGPLIY GIQEASAYYF NKRPSQLTTE ESIFLASIIP KPKHFRSSFA ENGKLKESME
     GYYKLIAGCL AQKGLISEIE ADTIRPEIQV TGDALNSLAG KTPESSSPTA EEQ
//