ID E0RSP6_SPITD Unreviewed; 619 AA.
AC E0RSP6;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:ADN02033.1};
GN OrderedLocusNames=STHERM_c10880 {ECO:0000313|EMBL:ADN02033.1};
OS Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=665571 {ECO:0000313|EMBL:ADN02033.1, ECO:0000313|Proteomes:UP000001296};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 6192;
RA Angelov A., Mientus M., Wittenberg S., Lehmann R., Liesegang H., Daniel R.,
RA Liebl W.;
RT "The genome sequence of Spirochaeta thermophila DSM6192.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADN02033.1, ECO:0000313|Proteomes:UP000001296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1
RC {ECO:0000313|Proteomes:UP000001296};
RX PubMed=20935097; DOI=10.1128/JB.01023-10;
RA Angelov A., Liebl S., Ballschmiter M., Bomeke M., Lehmann R., Liesegang H.,
RA Daniel R., Liebl W.;
RT "Genome sequence of the polysaccharide-degrading, thermophilic anaerobe
RT Spirochaeta thermophila DSM 6192.";
RL J. Bacteriol. 192:6492-6493(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CP001698; ADN02033.1; -; Genomic_DNA.
DR RefSeq; WP_013313874.1; NC_014484.1.
DR AlphaFoldDB; E0RSP6; -.
DR PaxDb; 665571-STHERM_c10880; -.
DR KEGG; sta:STHERM_c10880; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_1_2_12; -.
DR Proteomes; UP000001296; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
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 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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..228
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 260..588
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 619 AA; 68373 MW; 12CADB32CD898653 CRC64;
MKVKEYGKTS SNQRISILIA LSVVIVFLYI GRLFSVQVVE NELFSAQSQK TIQRAVLIPA
RRGDVFARDY RSILATSRDS FTLLFFRSEV GKEQLPPLVD RLGGHLGVSA RSLLDKIESS
ASDPVVLAQG VGYEQIVGIA EHLSEFPGIG WQREPSRYYP YGDLFAHVVG YIGEITQEEL
TALYNKGYTQ GTLIGKSGVE KVYDELLRGK TGLKHRIVDA SGQILDEQVV FFPENGKTLV
LTLDPAIQTL IKKALGPRNG AIVVLKPSTG EILGLYSYPS YDSNLLYDPK EGRAYFTRLS
LDKSFPFINR AIQSSYAPAS TFKIVMTAAV LMEKVFPPDR TIVCRGEYRY GDRVFKCWKE
AGHGPLALED ALAQSCDVYF YTVGAEYLGV DRIAAYAKEF GLGEPTGIDL PGEVRGIVPT
PRWKMETYNY PWVGGDTVNM SIGQGFLSVT PLQLADVVAS VVNGGFIMRP HVLKEVRDPT
TGEVLEDISP SLLRTSNITE DVFSSVRAAM RGVVTHGTAL PVITTPIVEV AGKTGTGEVG
LENRYTSWFV GYAPYDALDP EEVVVVSVLV EATNDWEWWA PKAANIVFHG IFSGLSYEDT
VRELRQGPAR WYLPALEDR
//
