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Database: UniProt
Entry: A0A1M6A9P5_9BACT
LinkDB: A0A1M6A9P5_9BACT
Original site: A0A1M6A9P5_9BACT 
ID   A0A1M6A9P5_9BACT        Unreviewed;       623 AA.
AC   A0A1M6A9P5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Zn-dependent protease with chaperone function {ECO:0000313|EMBL:SHI33181.1};
GN   ORFNames=SAMN02745146_0557 {ECO:0000313|EMBL:SHI33181.1};
OS   Hymenobacter daecheongensis DSM 21074.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1121955 {ECO:0000313|EMBL:SHI33181.1, ECO:0000313|Proteomes:UP000184418};
RN   [1] {ECO:0000313|EMBL:SHI33181.1, ECO:0000313|Proteomes:UP000184418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21074 {ECO:0000313|EMBL:SHI33181.1,
RC   ECO:0000313|Proteomes:UP000184418};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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}.
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DR   EMBL; FQYN01000001; SHI33181.1; -; Genomic_DNA.
DR   RefSeq; WP_073104997.1; NZ_FQYN01000001.1.
DR   AlphaFoldDB; A0A1M6A9P5; -.
DR   STRING; 1121955.SAMN02745146_0557; -.
DR   OrthoDB; 9789270at2; -.
DR   Proteomes; UP000184418; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07328; M48_Ste24p_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR   PANTHER; PTHR43221:SF1; PROTEASE HTPX; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SHI33181.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184418};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        28..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          144..331
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   623 AA;  68558 MW;  9794573B4F6C7409 CRC64;
     MTREEFLARL RRLSPLAEAN PAGYRRRVWL WALLGYAGIL LLLLGTVGLL LLTLAVGVFS
     KAFAIVFKVG AVLAVFAWKV LRSLWVKFDP PEGLPLTPAE AAPLLALLQQ QTQALRAPQV
     HQVLLTADFN AAAVQVPRLG VLGWPRNYVV VGLPLLQSLS PVQAAAVVGH ELGHLRGGHG
     RFGAWIYRVS QTWTQLIEQL ERQSNRSLFS RFTAWYVPRF NAWSHPVRRT DEFAADAAAA
     QLTSPQAMAE ALCATVVRDA TLDRLHWNVL SASLAERPTP PSDAISRLLP LAKNSRLPAA
     DEQILLANAN EAEPDLFSTH PTLGERLAAL GQAAAVPPLP ATTAAEAWLG ASLPALAAAL
     DEAWVSSRAA IWQERHSLLR QQQERLRELT TQQQAGASLT ADESWELADL TEDHISSTEA
     LPLFQQLTDD ARWKLPARFS VGRILLNSDN AEGLTWLAAV MEQEPNYMAP GLALQEAYYQ
     RQGNREQVRK LGAVQLRHAD TLDEAVAERE AIRPADTLLP HGLTEEELQK LRAELAVPEY
     AIGRAWLMRK QVQYFIQKPL YVLLVARLST AAGSSKEAPE TWVQELAAKI ELPGEGFVIA
     IGKDFAWLER AARQQAAAEV FVA
//
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