ID A0A377KKE1_9ENTE Unreviewed; 730 AA.
AC A0A377KKE1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:STP29639.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:STP29639.1};
GN Name=pbpX {ECO:0000313|EMBL:STP29639.1};
GN ORFNames=NCTC8129_01845 {ECO:0000313|EMBL:STP29639.1};
OS Enterococcus durans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=53345 {ECO:0000313|EMBL:STP29639.1, ECO:0000313|Proteomes:UP000254070};
RN [1] {ECO:0000313|EMBL:STP29639.1, ECO:0000313|Proteomes:UP000254070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC8129 {ECO:0000313|EMBL:STP29639.1,
RC ECO:0000313|Proteomes:UP000254070};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; UGIF01000002; STP29639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A377KKE1; -.
DR Proteomes; UP000254070; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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 CDD; cd06576; PASTA_Pbp2x-like_1; 1.
DR CDD; cd06575; PASTA_Pbp2x-like_2; 1.
DR Gene3D; 2.20.70.70; -; 1.
DR Gene3D; 3.30.70.2110; -; 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; IPR005543; PASTA_dom.
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; PF03793; PASTA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 2.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 2.
DR PROSITE; PS51178; PASTA; 2.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:STP29639.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transferase {ECO:0000313|EMBL:STP29639.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 614..674
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 675..730
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 730 AA; 81050 MW; F9B468BE3FB0590D CRC64;
MSLKNKFRRF MEKKNLNPMN NRKKVGIILF ATSIGLFFLF AVRFSYIVIG GHVAGTSLAE
KTEQLYKGSE VVKAKRGTIY DRNGVALAED AKSYSIKAIL SKTYTTGDKK LYAQEKDFDK
IATILHKNLS IEKSQALKIL QDGAKNELYQ VEFGNYGKNI SQETRQTIES EMKKENIAGL
YFEDHSARMY PNGVFSSHFI GYAVPNKDDT GLVGKLGLEA AYNDVLSGKN GEIIYQKDNY
QNALPGTVAE EEKAVNGQDI YTTLDSRLQS YLETLMDQVN DEYQPEELTA VLMKAKTGEI
LAMGQRPTFN PETMEGLQEK DSVWRNFLVQ DSYEPGSTMK VFTTAAAIEE GKFNENETYQ
SGKIKVADAT INDHDYGAKG VLTMRQALSW SSNVGMVMLE QRMGGAWYNY LQKLGFGQST
HSGLDDEVSG ALPTENIVDR AMSAYGQAVG VTNFQMMKAF TSIANNGTMI QPRYISKIVD
PTTGEERATQ TEVLGQPFSK ETTQKVREYM RDVVESENYG SAYGVYSVPG YNVSAKTGTA
QIASDTGGYQ TGETAYLYSI VEMVPSEDPE YVLYLTMKHP KTYDRDALAK IANPLMKRAM
DFKETETDEK TEEATEKVTV ADYRNLGTDV AAADAQKSGL QPIVIGDGKK VKKQSTEQGD
QLISGEKIIL YTGGEKLMPD VTSWSKADIM KLGKILGIEV TFDGDGYCTK QGLAPYEKIT
DDKLSFTLEE
//
