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Database: UniProt
Entry: A0A1C1A318_9BACL
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ID   A0A1C1A318_9BACL        Unreviewed;       291 AA.
AC   A0A1C1A318;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Zn-dependent protease {ECO:0000313|EMBL:OCT14938.1};
GN   ORFNames=A8709_12465 {ECO:0000313|EMBL:OCT14938.1};
OS   Paenibacillus pectinilyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=512399 {ECO:0000313|EMBL:OCT14938.1, ECO:0000313|Proteomes:UP000093309};
RN   [1] {ECO:0000313|Proteomes:UP000093309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC13222 {ECO:0000313|Proteomes:UP000093309};
RA   Zhang J., Zhang X.;
RT   "Paenibacillus oryzae. sp. nov., isolated from the rice root.";
RL   Submitted (MAY-2016) 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:OCT14938.1}.
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DR   EMBL; LYPC01000014; OCT14938.1; -; Genomic_DNA.
DR   RefSeq; WP_065851783.1; NZ_LYPC01000014.1.
DR   AlphaFoldDB; A0A1C1A318; -.
DR   STRING; 512399.A8709_12465; -.
DR   Proteomes; UP000093309; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06161; S2P-M50_SpoIVFB; 1.
DR   InterPro; IPR046342; CBS_dom_sf.
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; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:OCT14938.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000313|EMBL:OCT14938.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093309};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..102
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   291 AA;  32671 MW;  DD997EFB7EF4B6BB CRC64;
     MIKIAGTKYR FHPLFTLIMI GCALTGYFLE AITLFGIVLI HELGHLTAAK GFGWRVQEVQ
     LLPFGGVLIV DEMGTTSTKE ELVVALAGPL QHVWMILLAV VIKSFDMGSS SWWDYFIQAN
     LMIGLFNLIP VMPLDGGKVM QGLLSYIMSY HNAIVYSTWI SMILSVSIIV MAITQLLHGQ
     LPINILVVGI FLLISNWYAY RQIPYHFLRF LMGRGFRVGQ LLSRGTRAQP IVITKQLTMA
     ETLKLFMREK YHLIYVVNEV GRIQAVLPEQ QIVGGYLDGK KPGSAVSDLF M
//
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