ID A0A1D8GC35_9CLOT Unreviewed; 675 AA.
AC A0A1D8GC35;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Stage V sporulation protein D {ECO:0000313|EMBL:AOT68467.1};
GN ORFNames=Gferi_01980 {ECO:0000313|EMBL:AOT68467.1};
OS Geosporobacter ferrireducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Geosporobacter.
OX NCBI_TaxID=1424294 {ECO:0000313|EMBL:AOT68467.1, ECO:0000313|Proteomes:UP000095743};
RN [1] {ECO:0000313|EMBL:AOT68467.1, ECO:0000313|Proteomes:UP000095743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRF9 {ECO:0000313|EMBL:AOT68467.1,
RC ECO:0000313|Proteomes:UP000095743};
RA Kim S.-J.;
RT "Genomic analysis reveals versatility of anaerobic energy metabolism of
RT Geosporobacter ferrireducens IRF9 of phylum Firmicutes.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP017269; AOT68467.1; -; Genomic_DNA.
DR RefSeq; WP_069974036.1; NZ_VENK01000003.1.
DR AlphaFoldDB; A0A1D8GC35; -.
DR STRING; 1424294.Gferi_01980; -.
DR KEGG; gfe:Gferi_01980; -.
DR OrthoDB; 9804124at2; -.
DR Proteomes; UP000095743; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR CDD; cd06576; PASTA_Pbp2x-like_1; 1.
DR Gene3D; 3.30.10.20; -; 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 InterPro; IPR011927; SpoVD_pbp.
DR NCBIfam; TIGR02214; spoVD_pbp; 1.
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; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR PROSITE; PS51178; PASTA; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000095743};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 596..672
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 675 AA; 75494 MW; BAD4B3F94F1C0FB3 CRC64;
MSTPSIANKK RLVVLLFTVC FILFGLIFRI GWIQIVDGER YRQLAHMQQT RDIPIPAKRG
VVFDRKGKEL AISASTSTVW ARPAEVERSG KADEISKELA AILEKDEIEI KEKLTRKNVG
LIKIEKWIDK EKADAIRQAK MEGVWIAEDN RRHYPFGTFA AHILGHTTDD NRGLVGIELE
YDKYLSGLPG RWIKNTDAAG RQLPYGVEKY YKPENGLNVV LTIDEVIQHF TEKALDSTLA
QTQAKKVIAI VMDPKTGDIL AMATKPDFDP NSPRIPTSEE KKREFENLDT KEQQKLWNEM
WRNPMISDTY EPGSTFKLIT SAAGLEEGVV EPNSPFYCSG HITVAGQRIR CWRYYNPHGA
QTFTVGVQNS CNPVFIEIGQ RLGVENYYKY IEAFGFTKIT GVDLPGEGNA IVQSKERVGP
VELATISFGH GISVTPLQLV NAIAAIGNDG KLMKPRIVKE LVDDEGNVIH RYEPKMIRQA
VSEKTARELR LIMESVVTDG SGKSAYIPGY RIGGKTGTAD KIENGRYVSG KVYSSFVALA
PIDDPRLAVL VVVDEPQGVR FGSLTAAPAV HDILKDSLRY MDIEPQYNEK EAKQYAKEEV
TVPEVRNLTL KNAAKTLADR GLQYDTEPTT HGLQYDTEPT TAENPETIIV DQFPKPGAKV
PEKSIIILYL KRENP
//
