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Database: UniProt
Entry: A0A0L0W7H4_GOTPU
LinkDB: A0A0L0W7H4_GOTPU
Original site: A0A0L0W7H4_GOTPU 
ID   A0A0L0W7H4_GOTPU        Unreviewed;       433 AA.
AC   A0A0L0W7H4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Peptidase SpoIVB {ECO:0000313|EMBL:KNF07412.1};
DE            EC=3.4.21.116 {ECO:0000313|EMBL:KNF07412.1};
GN   Name=spoIVB {ECO:0000313|EMBL:KNF07412.1};
GN   ORFNames=CLPU_17c00370 {ECO:0000313|EMBL:KNF07412.1};
OS   Gottschalkia purinilytica (Clostridium purinilyticum).
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Gottschalkiaceae;
OC   Gottschalkia.
OX   NCBI_TaxID=1503 {ECO:0000313|EMBL:KNF07412.1, ECO:0000313|Proteomes:UP000037267};
RN   [1] {ECO:0000313|Proteomes:UP000037267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1384 {ECO:0000313|Proteomes:UP000037267};
RA   Poehlein A., Schiel-Bengelsdorf B., Bengelsdorf F.R., Daniel R., Duerre P.;
RT   "Draft genome sequence of the purine-degrading Gottschalkia purinilyticum
RT   DSM 1384 (formerly Clostridium purinilyticum).";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNF07412.1}.
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DR   EMBL; LGSS01000017; KNF07412.1; -; Genomic_DNA.
DR   RefSeq; WP_050356252.1; NZ_LGSS01000017.1.
DR   AlphaFoldDB; A0A0L0W7H4; -.
DR   STRING; 1503.CLPU_17c00370; -.
DR   PATRIC; fig|1503.3.peg.717; -.
DR   OrthoDB; 9765242at2; -.
DR   Proteomes; UP000037267; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00989; PDZ_metalloprotease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008763; Peptidase_S55.
DR   InterPro; IPR014219; SpoIVB.
DR   NCBIfam; TIGR02860; spore_IV_B; 1.
DR   PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF05580; Peptidase_S55; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS51494; SPOIVB; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KNF07412.1};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00023049};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037267}.
FT   DOMAIN          196..432
FT                   /note="Peptidase S55"
FT                   /evidence="ECO:0000259|PROSITE:PS51494"
SQ   SEQUENCE   433 AA;  48057 MW;  8D937FBE5C76CF47 CRC64;
     MTKNLRQKKL VFFILILALI VPYSVQILNV LHYPSQIDIT RGGSQRLDVL FPFTLEILEN
     KKVLELSNKH EEKIRIKNSY HFKPSENGIA KVAINFLGFL PIKHVNVNVI DDIYLTPGGE
     ALGVKLNTKG VLVVGMSEIE NVNGEKSNPA ADAGIKVGDS VTKINGKKIK DANQVIDILN
     NAKNEKLNIT IERDSKEMVK EVTPIKSKQD NSYRLGIWVR DKTAGIGTLT FYDEKSKKFG
     ALGHSITDVD TGTLMSIENG EIMEAEISSI EQGKKGTPGE IRGMFFENNK VLGKITSNTS
     FGIYGAMYKN LSDKKRLPIA LQNEVQIGKA HILTTIENSK VEKYEVEILK KENQLNPETK
     SMVIKVTDKR LLNKTGGIVR GMSGSPIIQN GKIIGAVTHV FVNDPTKGYG LYIEWMMKEA
     GIPFKSNNLA NNK
//
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