ID Q8XMX4_CLOPE Unreviewed; 728 AA.
AC Q8XMX4;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Stage V sporulation protein D {ECO:0000313|EMBL:BAB80270.1};
GN Name=spoVD {ECO:0000313|EMBL:BAB80270.1};
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB80270.1, ECO:0000313|Proteomes:UP000000818};
RN [1] {ECO:0000313|EMBL:BAB80270.1, ECO:0000313|Proteomes:UP000000818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818};
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; BA000016; BAB80270.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8XMX4; -.
DR SMR; Q8XMX4; -.
DR STRING; 195102.gene:10489821; -.
DR KEGG; cpe:CPE0564; -.
DR HOGENOM; CLU_009289_6_0_9; -.
DR Proteomes; UP000000818; 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 CDD; cd06575; PASTA_Pbp2x-like_2; 1.
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 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; 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; 2.
DR PROSITE; PS51178; PASTA; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000818};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 604..664
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 668..728
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 728 AA; 79690 MW; 131353AE9B8E9418 CRC64;
MKRSYRDMAI IRKRLSFILA FIIIMCFILS IRLSYVMIVK GPEYAELAVE QWTNEVKISA
RRGKILDRDL NELAVSSNVY RVDFNLNAIR SYTKKTGKTN EELALEISKV LEMDKDTVLK
KLEFKLPSGA PAGAAILARR IEKEKADKVK ELEIPGVMVS PDTQRYYPND NFLSHVLGTT
NSDGVGLNGI ELKYDRVLSG SPGLKITEMV KDGAEYPYTI SRFTAPVDGK DVVLTIDEKL
QYFAEQIAEI GLIHHNADAA SVIIMNPNNG EILAMSNKPD FNPNKPYDGA ENFSGNTSSD
RIQKMWRNRS VSDSFEPGSI FKIITASAAV QEGVAGKDET YTCSGGLQKG DRFIKCWKRG
GHGTQTFEEI IQNSCNVGFM NLGEKLGAEK LNEYIKKFGL GKKSGVDLPG ESPGIVKKTE
NITDMDLATI SFGQTNTVNP IQFMTAVNAV ANGGTLIQPH VVKEISYINE NNDRVIDETF
VPKKTENLIS KETADQIKLA LENAVKNGSA KGAYKEGYGV AGKTGTAQKV NPETGGYGGG
YVASFVGFAP YDNPQISVMV SVDNPKNGEY YGGRVAAPLA GMLLQNIFNY IDLTEFHLDE
KLPEKETVII PEVRGLPIND TTSMLKELGI SYEIEGEGEF IVESNPAPGY PISPDTKITL
IAGDSSNLNS DVIIPDFKNY SKESAEKLLN QLGLIGEFVG EGPSVTKQSI SPDEVVNGNS
KITLTLGY
//