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Database: UniProt
Entry: A0A0Q4RQW2_9BACL
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ID   A0A0Q4RQW2_9BACL        Unreviewed;       461 AA.
AC   A0A0Q4RQW2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=SpoIVB peptidase {ECO:0000313|EMBL:KQO17489.1};
GN   ORFNames=ASF12_02025 {ECO:0000313|EMBL:KQO17489.1};
OS   Paenibacillus sp. Leaf72.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736234 {ECO:0000313|EMBL:KQO17489.1, ECO:0000313|Proteomes:UP000051722};
RN   [1] {ECO:0000313|EMBL:KQO17489.1, ECO:0000313|Proteomes:UP000051722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf72 {ECO:0000313|EMBL:KQO17489.1,
RC   ECO:0000313|Proteomes:UP000051722};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQO17489.1, ECO:0000313|Proteomes:UP000051722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf72 {ECO:0000313|EMBL:KQO17489.1,
RC   ECO:0000313|Proteomes:UP000051722};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQO17489.1}.
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DR   EMBL; LMLV01000001; KQO17489.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q4RQW2; -.
DR   STRING; 1736234.ASF12_02025; -.
DR   Proteomes; UP000051722; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR008763; Peptidase_S55.
DR   InterPro; IPR014219; SpoIVB.
DR   NCBIfam; TIGR02860; spore_IV_B; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF05580; Peptidase_S55; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51494; SPOIVB; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051722};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        27..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          218..457
FT                   /note="Peptidase S55"
FT                   /evidence="ECO:0000259|PROSITE:PS51494"
SQ   SEQUENCE   461 AA;  49623 MW;  110770FCE87A40DD CRC64;
     MAINPLSSCD GITGSVKSLN SSKRKRWFGL VLVILICMVG FSTPFQHLAS IPNELRLFTG
     QSKRLQYGVP VHAQVTVDPR MLQVNGSSTR SLSVNLNEPL SLHSQQSGET RMKVKLFGKI
     PFKTVKVNVV PDLKVIPGGQ TIGVKVKSAG ILVVGHHQVT SQNGSKQSPG ELAGLRLGDL
     IVKINGQKVS EVRKVAELVD HAGNNKKALD IVYKRGGHLG KTVLNPSYDA EDRTWRLGLY
     IRDSAAGVGT LTFYAPDQGV YGALGHVITD MDTQTAIEVG DGQILQSSVT SINKSQNGEP
     GEKRAHFVKE SKVLGNVERN TPFGIFGKMN ENPTHSYNSN AMPVAFAEEV AEGTAQIYTV
     VNGQKVEKFD IEIAHVMKQN SPATKGMVIK ITDKRLLDKT GGIVQGMSGS PIIQNGKLVG
     AVTHVFVNDP TSGYGCFIEW MLQDAGVLLK STLQQGSQTA A
//
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