ID D3FTZ6_ALKPO Unreviewed; 413 AA.
AC D3FTZ6;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Processing protease {ECO:0000313|EMBL:ADC51977.1};
GN OrderedLocusNames=BpOF4_19690 {ECO:0000313|EMBL:ADC51977.1};
OS Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS (Bacillus pseudofirmus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX NCBI_TaxID=398511 {ECO:0000313|EMBL:ADC51977.1, ECO:0000313|Proteomes:UP000001544};
RN [1] {ECO:0000313|EMBL:ADC51977.1, ECO:0000313|Proteomes:UP000001544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2126 / JCM 17055 / OF4
RC {ECO:0000313|Proteomes:UP000001544};
RX PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA Hu F.Z., Krulwich T.A.;
RT "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT support the ability to grow in an external pH range from 7.5 to 11.4.";
RL Environ. Microbiol. 13:3289-3309(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP001878; ADC51977.1; -; Genomic_DNA.
DR AlphaFoldDB; D3FTZ6; -.
DR STRING; 398511.BpOF4_19690; -.
DR MEROPS; M16.A15; -.
DR KEGG; bpf:BpOF4_19690; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_3_0_9; -.
DR Proteomes; UP000001544; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ADC51977.1};
KW Protease {ECO:0000313|EMBL:ADC51977.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001544}.
FT DOMAIN 13..159
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 167..338
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 413 AA; 46386 MW; CAB6F7FC0844ED2B CRC64;
MIQKIELDNG VRIMAEAIPT VRSVSIGVWI GTGSRYEEVH ENGISHFLEH MFFKGTKKRS
AADIAEAFDK IGGQVNAFTS KEYTCYYAKV LDEHAPIAVD VLSDMFFNSE FEAKELQKER
NVVLEEIKMV DDTPDDIVHD LLSKAAYGEH SLGYPILGTQ DTLKTFDEKA LRSYMDRYYT
GDHVVISIAG NITDEVIQSI KDIFKEVKPT TYQYEASAPR FQSELITRKK ETEQAHLCLA
YPGLEIGNKD VYSLILLNNL LGGSMSSRLF QEIREKRGLC YSVFSYHSSY QDSGMLTVYA
GTALEQLDEL VVALNQTTSR LCEAGMNEKE LQNGKEQLKG SLMLSLESTN SRMSRNGKNE
LMLKRHRTLD DILAEINNVT LENVNRLAQT LLSTEPAISL ISSTGEVPKS LRA
//
