ID A0A399G5L9_9ACTN Unreviewed; 581 AA.
AC A0A399G5L9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:RII03807.1};
DE Flags: Fragment;
GN ORFNames=NI17_03955 {ECO:0000313|EMBL:RII03807.1};
OS Thermobifida halotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=483545 {ECO:0000313|EMBL:RII03807.1};
RN [1] {ECO:0000313|EMBL:RII03807.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:RII03807.1};
RA Toth A., Tancsics T.A., Farkas T., Papp P., Olasz F., Balint B.,
RA Herczeg R., Nagy I., Baka E., Kukolya J.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2014) 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:RII03807.1}.
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DR EMBL; JRUV01000136; RII03807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399G5L9; -.
DR STRING; 483545.GCA_001660385_03834; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.450.330; -; 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; 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 Transferase {ECO:0000313|EMBL:RII03807.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 56..207
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 253..558
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RII03807.1"
SQ SEQUENCE 581 AA; 62469 MW; 865339BE71B84A6D CRC64;
RRPFRRRAPQ PRIRIMGAIL GVVLLLFAVR LVQIQGIDAD DYAEAAANLR LATIEIPTVR
GDITDASGRP FAMSVEVRTV FVDPAEVRAD QRDEVVRELS QRFDLSAEEV AARLDARVDG
QPSRYEVVQR GVSVEEWEEL DALGLHGVSA ERAYKRVYPE QTGAANLVGF VGTEGYGLEG
LEAVLDSTLA GEAGQQQVEV GSDGTQIPMA GGLVKEPVPG RTVRLTLDMD LQWYAQQALA
ERAEELGAEA GNVVVMTRDG QIKAMANYPT YDPNDFASAT AEQRRNGAVA DAFEPGSTNK
AITVAAALEE GVTTPDTVYT VPDSIRRHDL EFRDSHPHPT QRLTVNGIMA TSSNVGAIQI
AEELGAEKMY EYLRRFGFGQ PTGLDLPGEN AGILTDPQHW SGTDLPSISF GHSVSVNAVQ
LAGVYAIVAN DGIRVEPTLV AGTVDPDGEF TAAPEPESER VISADTAADL RLMLEGTTGE
MGTARQARID GYRIGGKTGT ANRINPETGT YQGGGYVSSF VGIAPVDDPE LVVLVVLHNP
QEEYYGGEAA TPVFTDVMSF ALKTMQVPPT GTEAPKLRME E
//