ID A0A117M538_9FIRM Unreviewed; 726 AA.
AC A0A117M538;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:KUK84822.1};
GN ORFNames=XE00_0513 {ECO:0000313|EMBL:KUK84822.1};
OS Desulfofundulus kuznetsovii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfofundulus.
OX NCBI_TaxID=58135 {ECO:0000313|EMBL:KUK84822.1, ECO:0000313|Proteomes:UP000054111};
RN [1] {ECO:0000313|Proteomes:UP000054111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK84822.1}.
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DR EMBL; LGGU01000012; KUK84822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117M538; -.
DR PATRIC; fig|58135.3.peg.2; -.
DR Proteomes; UP000054111; Unassembled WGS sequence.
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 CDD; cd06575; PASTA_Pbp2x-like_2; 1.
DR CDD; cd06577; PASTA_pknB; 1.
DR Gene3D; 3.30.10.20; -; 2.
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; 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; 2.
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; 1.
DR PROSITE; PS51178; PASTA; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:KUK84822.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 600..660
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 666..725
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 726 AA; 78347 MW; F35620AA12150CAD CRC64;
MPDLDPAKKS FTTKRVALVF ILISLALFGL VSRLFWVQAV WGPGLKRQAE EYHTQDVTVQ
PERGSIYDRN HNELVTNIPA FSVYAQSKKI KDPAGLSEKI APVLGIKQAL VYEKLCSKEP
FIWLTHNLEY SAAERLKNLS KELGGNPDKD SKKDPDLQWI GLIESNKRSY PQGSMAAHLL
GFVGSDNQGL TGLENSYDSY LKGKPGSSTI ESDAKGLPVP QAQTDVNPSD PGANLVLTID
QTIQFFVERE LDNLVASYKP ARAAIIVMDP ATGQILAMGN RPAFNPGNWS KEPESVWGGD
TAVLYNYEPG STLKMFIAAA ALEKRFVSPG ERLYDPGSIV VKGRRIYCAE REGHGSLTFS
EAVSVSCNVA LIQVGQRLGK ENIYKYLQEF GFGARTGIDL PGEESGVLMD KKKATELDLA
TMSIGQSIAV TPIQLITGAC AIANGGKLMK PYLVKALEDD QRKIVKEFKP QEVRSIISSE
TARTLTSMME DVILEGTGTK AQVEGYRIAG KTGTAQIPGP KGYIEGKYVA SFLGYGPLDN
PRAAVLVIVD EPKGSKYHGG EVAAPAFQSV MRDTLVYLGI PQEKTGAQKS EEELPDPSKV
PSRVAVPNVI GFPAEQATRL IKNRGLVCWA SAPQGVISGQ KPGGGSNLIK GSLVTLKVTP
FDLSKPPDKI TVPDLKSLTL KKAAVLLEEI GLKLKAEGSG LALYQSPPAG TGVKPGSVVK
VYFNPE
//