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Database: UniProt
Entry: A0A268E1K5_9BACI
LinkDB: A0A268E1K5_9BACI
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ID   A0A268E1K5_9BACI        Unreviewed;       288 AA.
AC   A0A268E1K5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Stage IV sporulation protein FB {ECO:0000313|EMBL:PAD66996.1};
GN   ORFNames=CHH83_21105 {ECO:0000313|EMBL:PAD66996.1};
OS   Bacillus sp. 7586-K.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2021690 {ECO:0000313|EMBL:PAD66996.1, ECO:0000313|Proteomes:UP000216230};
RN   [1] {ECO:0000313|EMBL:PAD66996.1, ECO:0000313|Proteomes:UP000216230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7586-K {ECO:0000313|EMBL:PAD66996.1,
RC   ECO:0000313|Proteomes:UP000216230};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family.
CC       {ECO:0000256|ARBA:ARBA00007931}.
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:PAD66996.1}.
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DR   EMBL; NPCL01000110; PAD66996.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A268E1K5; -.
DR   OrthoDB; 166377at2; -.
DR   Proteomes; UP000216230; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06161; S2P-M50_SpoIVFB; 1.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR39188; MEMBRANE-ASSOCIATED ZINC METALLOPROTEASE M50B; 1.
DR   PANTHER; PTHR39188:SF3; ZINC METALLOPROTEASE SLR1821-RELATED; 1.
DR   Pfam; PF02163; Peptidase_M50; 2.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216230};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        117..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          33..106
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
FT   DOMAIN          115..167
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   288 AA;  33878 MW;  CB0451512B4555F6 CRC64;
     MTKYLTLLQK VHIHPLLWVM IGISVITASF KPLMMLMLIV FIHEMGHAIS AHFFSWRIKS
     IMLLPFGGVA EVDEHGNRSL KQELIVVLAG PSQHVWLQGV AYVLYQMNFL NIADYQMFTF
     YNLSILLFNL LPIWPLDGGK LLFIVFSHLW AYKKAHMYML LTSSFFLTVY LVFTLIISPT
     HINMWIIIIF LLYSLYDEYK NRMYGCLRFL MERYYGKQNT IHQLKPIVVD ESDLIYHVLL
     QFQRGCKHLI VVEKNGRKIA EMDENELLHA YFANKLIDSR VGDLHYVY
//
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