ID   A0A1M7EZG5_9FIRM        Unreviewed;       711 AA.
AC   A0A1M7EZG5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Stage V sporulation protein D (Sporulation-specific penicillin-binding protein) {ECO:0000313|EMBL:SHL97056.1};
GN   ORFNames=SAMN02746066_00298 {ECO:0000313|EMBL:SHL97056.1};
OS   Anaerosporobacter mobilis DSM 15930.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerosporobacter.
OX   NCBI_TaxID=1120996 {ECO:0000313|EMBL:SHL97056.1, ECO:0000313|Proteomes:UP000184038};
RN   [1] {ECO:0000313|EMBL:SHL97056.1, ECO:0000313|Proteomes:UP000184038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15930 {ECO:0000313|EMBL:SHL97056.1,
RC   ECO:0000313|Proteomes:UP000184038};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FRCP01000005; SHL97056.1; -; Genomic_DNA.
DR   RefSeq; WP_073282018.1; NZ_FRCP01000005.1.
DR   AlphaFoldDB; A0A1M7EZG5; -.
DR   STRING; 1120996.SAMN02746066_00298; -.
DR   OrthoDB; 9804124at2; -.
DR   Proteomes; UP000184038; 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:UP000184038};
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          68..227
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          272..598
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          609..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..632
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..663
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..682
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..711
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   711 AA;  79641 MW;  DABFBA3CF7F933F6 CRC64;
     MNRRDRVKEK KMKKFTHQMQ AKTLLVFGVV LLLLIILVAR LTYLRNENGD RYSKKVLSQQ
     TYSSSVIPYR RGDIVDRNGT VLATSIKVYN LILDPKTILE TKKVNGEVTT PYREPTLQAL
     TTYFDVEYDE LNQILIDKPK NQYTVMLKQL EYNEIKDFKE AMAKEDSKIQ GVWFEEEYKR
     IYPYNSTASD IIGFTSSGNV GNWGLEQTYN SYLNGTNGRE YGYFDSELNL ERTVKPAVDG
     DTVVSTIDLN IQQIVEKHIK KFMKDIGAKN TAVIVMDPNT GEIISMASDK QYDLNDPYDL
     TGYYTDSEIK KMSEEERLNA LYDIWKNFAI SQNYEPGSTF KPFVMAAALD EAIVSDGDHF
     YCDGGEVVVE GTKRIRCVNR SGHGDLTIEE AIMKSCNDTM MQVVAKMGRS LMSKYQFNYG
     FGRKTGIDLP GEEKGQVFTE DQLNPLELAT TSFGQGLTTT MVQMASSLSA TINGGYYYTP
     HLVNKVKNAD GATVENKDAV LSKQVISTKT SDLLRRYLYN TVEKGTAVTA GVKGYQIGGK
     TGTAEKHTGD EGAYLVSFIG YVPYDNPQYV IYTIVDEVNA DDQAQSRYAQ QLSHDILEEI
     LPFLGVLKSS DDSTTEDKDK TDKKDTTDKK DDASNSSQTN GTNANDANAD NTNQANEATS
     GEQNVESGED EENDTENYDF FDDDVDSQIK NGLDSSKSDE EEKGPATEGE E
//