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Database: UniProt
Entry: A0A1M4W9T1_STRHI
LinkDB: A0A1M4W9T1_STRHI
Original site: A0A1M4W9T1_STRHI 
ID   A0A1M4W9T1_STRHI        Unreviewed;       625 AA.
AC   A0A1M4W9T1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Zn-dependent protease with chaperone function {ECO:0000313|EMBL:SHE77969.1};
GN   ORFNames=SAMN05444320_1011062 {ECO:0000313|EMBL:SHE77969.1};
OS   Streptoalloteichus hindustanus.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Streptoalloteichus.
OX   NCBI_TaxID=2017 {ECO:0000313|EMBL:SHE77969.1, ECO:0000313|Proteomes:UP000184501};
RN   [1] {ECO:0000313|EMBL:SHE77969.1, ECO:0000313|Proteomes:UP000184501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44523 {ECO:0000313|EMBL:SHE77969.1,
RC   ECO:0000313|Proteomes:UP000184501};
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; FQVN01000001; SHE77969.1; -; Genomic_DNA.
DR   RefSeq; WP_073480080.1; NZ_FQVN01000001.1.
DR   AlphaFoldDB; A0A1M4W9T1; -.
DR   STRING; 2017.SAMN05444320_1011062; -.
DR   OrthoDB; 155290at2; -.
DR   Proteomes; UP000184501; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:SHE77969.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184501};
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        41..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          136..306
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   REGION          588..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   625 AA;  67357 MW;  3251A50A504A145F CRC64;
     MRSPWRAVLA LTVLVGFFAC AAVLAAGLAG AALYAMADGD IGMTAIELLL CSALLGTAVG
     LFLPPVLRVR HRARGHVVDR AAQPELWEVI DELAGIARSR PPDELRVVPG VRIAFWEDAP
     VLGLVPGHRC LEVGLPLLGG LTVAELRAVL AHELAHLGDR EGRPHAVAYR ATALVEQVVA
     DSEGDWRRPV LRAWGNLVLS VAAPVNQRQE QVADEAAVAA AGVEAACAAF RRMAALERAW
     SDYGQQYLAM APIARRTPDV LLGFRSYLSA PRRQREWAEL EDEALDAGPS GPHDRHAPLR
     ERIEAMRAAG GEEPEADDRP AWSLLTSPGR SVPELEDALL VDLGPRAPWP ELVRAAVVRK
     AEDAARRLSR AVLDSGVRVD GRAAQTTVAG VLLAVHRGLG CELVKPALDP GLAPGEVSAA
     SDALLVELLG GAVTAALCRT GRARPELNWD GPCWLRLASG QVVDVERLVG PAVRTPGLVP
     QLHRHLVRIG VPLDFAARPA EPPEPELVAS ANGVRCDGDP HDVRVYDSGL LVLPAGSPAR
     KPLPELRRRP GARWVCGHDV EWARLVHRQS GWDVWLQLRG GDELELTSAS DTAHDGDPQE
     GMARLLGDRL EVEDVRQRRR EPVHR
//
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