ID A0A1Y4S651_9FIRM Unreviewed; 741 AA.
AC A0A1Y4S651;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Peptidoglycan glycosyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B5E77_11945 {ECO:0000313|EMBL:OUQ25357.1};
OS Lachnoclostridium sp. An131.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965555 {ECO:0000313|EMBL:OUQ25357.1, ECO:0000313|Proteomes:UP000199743};
RN [1] {ECO:0000313|Proteomes:UP000199743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An131 {ECO:0000313|Proteomes:UP000199743};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUQ25357.1}.
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DR EMBL; NFLI01000013; OUQ25357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4S651; -.
DR Proteomes; UP000199743; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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:UP000199743};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 70..230
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 285..625
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 648..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..675
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 80884 MW; 2DAC1F86E38EA031 CRC64;
MSSKRKKRVR RQALLTNRVK NKLALLFAII VLALIGVNVR LAYINKTNGD KYTKRVLAQQ
DTNSILLPFR RGDILDRNGT ILATSEKVYN LVLDAKVLAE SAEQYPDRDY VGTTLQALAQ
CFDLDEAELR STYNENISSS YIVLLRKLTK DEISEFEALQ EDEETGTLIK GVWFEPGYIR
RYPYNTLACH VLGYTVTGNN VTGDVGQTGI EQEYNSVLNG TSGRSYKYLN EDLEQSTMVR
QPEDGHTVVS TIDATLQEIV EKYIDKFIED YTDKNVEGPA AKNIGVIMMN PQNGEILAMA
SDVDFDLNNP HDLVENGYLA QEQADAMTED ELLDARNQMW RNFCISDGYE PGSTVKPLTV
AAALELGVVS DSSTFLCDGG QVVVEGQPKI KCSKRAGHGI ITLEGALMFS CNDALMQIGA
KLGYENYLKY QEIFNFGLKT NIDLPGEANN ASTVFNEDTL GVTELATSSF GQGYNTTMIQ
VASAFSSVIN GGYYYQPHVV KKILDADGGT VETINATLVR QTVSEKTSSL VRQYLYHTMY
GEADSNGNNA TGRNARVAGY AMGGKTGTAQ KIPRSDRKYL VSFIGFAPVD NPQVVCYVVV
DEPNAASPEA QASSSFAQEI FKNIMTEAMP YLNIYATEEI PADMQDEVDA QKAAEEEAES
TEEGSEEETE EELPEGTLVD PNTGETVTMP TEEELAGEDG GDIMGGIESP ILPADGEEEG
DAGGGDSTAE ETGGGTDASQ E
//
