ID A0A1I0IR70_9FIRM Unreviewed; 708 AA.
AC A0A1I0IR70;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Stage V sporulation protein D (Sporulation-specific penicillin-binding protein) {ECO:0000313|EMBL:SET98887.1};
GN ORFNames=SAMN04487771_10953 {ECO:0000313|EMBL:SET98887.1};
OS [Clostridium] aminophilum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1526 {ECO:0000313|EMBL:SET98887.1, ECO:0000313|Proteomes:UP000199820};
RN [1] {ECO:0000313|EMBL:SET98887.1, ECO:0000313|Proteomes:UP000199820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1P1 {ECO:0000313|EMBL:SET98887.1,
RC ECO:0000313|Proteomes:UP000199820};
RA de Groot N.N.;
RL Submitted (OCT-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; FOIL01000095; SET98887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0IR70; -.
DR STRING; 1526.SAMN02910262_00742; -.
DR eggNOG; COG0768; Bacteria.
DR OrthoDB; 9804124at2; -.
DR Proteomes; UP000199820; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; 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 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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199820};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..229
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 276..603
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 638..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 78148 MW; 2221E5056E5E7B9A CRC64;
MKTSRNTKTK KLFRRYMQEK LAITVLTILV VLIILAVILY RLVSNKGVDY NQIVLGHQNY
ESRMIPYKRG SIIDRNGTYL ATSEKIYNMI LDPRQMNSDD GYNYVEPTID ALAECFSYDK
EELRQLIRDR ADSSYVVYKK LSGEEKAKFE EYKQKKNEEY RKATVDKGGK NRITGVWFED
HYKRVYPYNN LACNVIGFAL RDNNASGGVE QYYNDELTGV NGREFGYLND DTNPERTVKP
AVNGNTVKLT IDANLQNIVQ KYLDEWQTTT GSKVAACIMI DPRSGEILAM DTTTRFDLNN
PYDLSLYYSQ EEIDAMDEKT KADAWYKMWR NFCVNDTYEP GSPQKPFTVA GAMEEGTITG
NESYVCNGVM HIGDWDIHCD IRSGHGPLTV AQGIEKSCNV VMMSINQAQG VHNFLKHQAM
FGFGQKTNID LPGEADTSGL VYTEETMDVA SLATNSFGQN YNTTMIQMAS AFCSLVNGGS
YYRPHVVKEI LNDQGAVIRK NDPVLVRETV SENTSTFIKN ALALVVQSGT AKAAQIPGYQ
IGGKTGTAQK QPRSEKNYLV SFIGAVPIYD PQVVCYVVID TPNLPGEQQA HSTFASTVFQ
KIMAEALPYL NVFPEGGAGA AGDNAALAEQ SEGIIHSETT AAETPTNPDG SAATQGPSYD
EEFIEGGHAE ELPAEMPSGA SVEQAEDSAG ENDDAQAAAA QAAAMAPQ
//
