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Database: UniProt
Entry: A0A068LSS9_BACMM
LinkDB: A0A068LSS9_BACMM
Original site: A0A068LSS9_BACMM 
ID   A0A068LSS9_BACMM        Unreviewed;       429 AA.
AC   A0A068LSS9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=SpoIVB peptidase {ECO:0000313|EMBL:AIE60670.1};
DE            EC=3.4.21.116 {ECO:0000313|EMBL:AIE60670.1};
GN   Name=spoIVB {ECO:0000313|EMBL:AIE60670.1};
GN   ORFNames=BMMGA3_11370 {ECO:0000313|EMBL:AIE60670.1};
OS   Bacillus methanolicus (strain MGA3 / ATCC 53907).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=796606 {ECO:0000313|EMBL:AIE60670.1, ECO:0000313|Proteomes:UP000027602};
RN   [1] {ECO:0000313|EMBL:AIE60670.1, ECO:0000313|Proteomes:UP000027602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGA3 / ATCC 53907 {ECO:0000313|Proteomes:UP000027602};
RX   PubMed=25758049;
RA   Irla M., Neshat A., Brautaset T., Ruckert C., Kalinowski J., Wendisch V.F.;
RT   "Transcriptome analysis of thermophilic methylotrophic Bacillus
RT   methanolicus MGA3 using RNA-sequencing provides detailed insights into its
RT   previously uncharted transcriptional landscape.";
RL   BMC Genomics 16:73-73(2015).
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DR   EMBL; CP007739; AIE60670.1; -; Genomic_DNA.
DR   RefSeq; WP_034669252.1; NZ_CP007739.1.
DR   AlphaFoldDB; A0A068LSS9; -.
DR   STRING; 796606.BMMGA3_11370; -.
DR   KEGG; bmet:BMMGA3_11370; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_035713_0_0_9; -.
DR   OrthoDB; 9765242at2; -.
DR   Proteomes; UP000027602; Chromosome.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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   SMART; SM00228; PDZ; 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|PROSITE-ProRule:PRU00827,
KW   ECO:0000313|EMBL:AIE60670.1};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU00827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027602};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU00827}.
FT   DOMAIN          189..428
FT                   /note="Peptidase S55"
FT                   /evidence="ECO:0000259|PROSITE:PS51494"
FT   REGION          394..396
FT                   /note="PDZ binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00827"
FT   ACT_SITE        237
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00827"
FT   ACT_SITE        364
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00827"
FT   ACT_SITE        379
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00827"
SQ   SEQUENCE   429 AA;  46794 MW;  C3A9BCEABB19179E CRC64;
     MKYELLKKII GGILLVSLVA IGFSKPIQEY VNIPQKITLF EGQQFSLHKA VNVSAGLSAD
     NKSIALKQNR HSVSLQAKSY GKNEMILELA GLPIKKVDVD VLKDFKVIPG GQSIGIKLNT
     VGVLVVGHHQ IDTEKGKVSP GEIAGIKVGD IITEINGKRI KKMEDVAPIV QKTGNEGKPL
     DIVINRENEK MKTKLQPMKD KKEHIYKLGL YIRDSAAGIG TMTFYDPNSK KYGALGHVIS
     DMDTKKPIVV EDGQIVRSTV TSIEKGSNGN PGEKLARFST DREIIGNINR NSPFGIFGKL
     NRELKNGVMD KPLPIALSHQ VKEGPAQILT VVNEDEVSLF DIEIVSTIPQ KFPATKGMVI
     KVTDPKLLQK TGGIVQGMSG SPIIQNGKLV GAVTHVFVND PTSGYGVHIE WMLNEAGINI
     YEQPREKVS
//
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