ID   A0A1G5I8P3_9FIRM        Unreviewed;       753 AA.
AC   A0A1G5I8P3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Stage V sporulation protein D (Sporulation-specific penicillin-binding protein) {ECO:0000313|EMBL:SCY72317.1};
GN   ORFNames=SAMN02910371_03581 {ECO:0000313|EMBL:SCY72317.1};
OS   Butyrivibrio sp. INlla14.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=1520808 {ECO:0000313|EMBL:SCY72317.1, ECO:0000313|Proteomes:UP000199551};
RN   [1] {ECO:0000313|Proteomes:UP000199551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INlla14 {ECO:0000313|Proteomes:UP000199551};
RA   Varghese N., Submissions S.;
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; FMVS01000041; SCY72317.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5I8P3; -.
DR   OrthoDB; 9804124at2; -.
DR   Proteomes; UP000199551; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199551};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          69..225
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          275..627
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          660..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..690
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   753 AA;  83491 MW;  60CD2E06BA3855DC CRC64;
     MRQKKKKKPN GQKFTYGMRK KLLVLFVLVL MAFVGLGVRL ILITQNNGEE YERQVLSQQQ
     FDSTTLPFRR GEILDANGTI LAYSEKVYNL ILDAKLLLRD DKYLEPTLKA LVTEFELDGG
     QIRNYLSDHP TSQYYVLAKK LSYEQIADFQ EMITPGTEKY DENIQGVWFE SGYIRKYPNG
     SLACDIIGFT TGDNNGMYGL EEYYNDVLSG TTGREYGYID DDSNLERTTI PPTDGDSIVT
     TIDGNLQNIV EKYLQEFNDE YANNVREGNG ANNVGCIMMN VDTGEILAMS SYPFYDLNDP
     RDTSRLIGMP AVDEKGNKIK GESIYDSGVY ITEDMLSTFT SEQLYQNYNA LWKNFCITDT
     YEPGSVAKPF TVATGLETGA ITGNEVYNCT GSLEVGGWDI KCHNVYGDGQ VSVERGIEIS
     CNVAMMYIGQ SIGIDDFTKF QRQFGFGLKT NIDLAGEART EGLTYKSTDM VPTDLAVNTF
     GQGFNVDMIE MITAYCSLIN GGYFYEPHVV KKIVNSSGAT VKNIEPRVLR QTVSQSTSDK
     IIQYCEAVVM GDEGTGKTAR PAGYRIIGKT GTAQTLPRGN HQYVVSFMGA APADDPKIAV
     YVVVDRPNVA DQSTSTRLAT TLVRKILTEA LPYLNIPMTE ELSEKEQQEL AELREKMITP
     PLAEGAESSE AASTESSEEN IEEVEIQVEE TGDTEEKPAI WESFDVDPTT GYYIDPDTGN
     LLDPVNGSPS GSDELPDFGN DEKWNSSEGS SGE
//