ID S4A4K6_9ACTN Unreviewed; 527 AA.
AC S4A4K6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative zinc metalloprotease {ECO:0000313|EMBL:EPH45630.1};
GN ORFNames=STRAU_1331 {ECO:0000313|EMBL:EPH45630.1};
OS Streptomyces aurantiacus JA 4570.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=1286094 {ECO:0000313|EMBL:EPH45630.1, ECO:0000313|Proteomes:UP000014629};
RN [1] {ECO:0000313|EMBL:EPH45630.1, ECO:0000313|Proteomes:UP000014629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA 4570 {ECO:0000313|EMBL:EPH45630.1,
RC ECO:0000313|Proteomes:UP000014629};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Mueller M.;
RT "Draft Genome Sequence of Streptomyces aurantiacus, Which Produces
RT Setomimycin.";
RL Submitted (FEB-2013) 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:EPH45630.1}.
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DR EMBL; AOPZ01000050; EPH45630.1; -; Genomic_DNA.
DR RefSeq; WP_016639461.1; NZ_AOPZ01000050.1.
DR AlphaFoldDB; S4A4K6; -.
DR PATRIC; fig|1286094.4.peg.1310; -.
DR OrthoDB; 9781963at2; -.
DR Proteomes; UP000014629; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06164; S2P-M50_SpoIVFB_CBS; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR000644; CBS_dom.
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; PF00571; CBS; 1.
DR Pfam; PF02163; Peptidase_M50; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR PROSITE; PS51371; CBS; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Hydrolase {ECO:0000313|EMBL:EPH45630.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000313|EMBL:EPH45630.1};
KW Protease {ECO:0000313|EMBL:EPH45630.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014629};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 158..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 366..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 404..463
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 55289 MW; 2514FBCE6000D21C CRC64;
MDESGGSGRP QSEQAPARAE DAPAQAEDAP SSTSRPAPDH HSADDPRPAE SPTDPEAPHG
TGEDPGAPAS TPRPGTPDHR GDAAPDSAEP PAADHPAPAR PTTPVSVRKE HPADGDGDAD
RRDSAPPARA HAHHSGEPPK EQPKNPGGGL LMGRPFGVPV YVAPSWFLVA ALITWVFGGQ
LDRVLPELGS ARYLVSLFFA VAFYASVLVH ELAHTVAALR FKLPVRRIQL QFFGGVSEIE
KESETPGREF VLAFVGPLLS LVLAGVFYAG MRAVEPGTVP GVLLAGLMIS NLIVAAFNLL
PGLPLDGGRM LRAVVWKITG KPMSGTIAAA WVGRALAISV LVGLPILNQS GALGGETQDI
GGMDTVTDAL LAAILAAIIW TGAGNSLRMA RLREHLPELR ARALTRRAVP VETDTPLSEA
LRRANAAGAR ALVVVDPDGD PLSVVREAAI VGVPEHRRPW VAVSGLAQDI TEGMRIPAEL
AGEELLDRLR STPATEYLVV ETSGEIYGVL SAADVERAFV KAMARPN
//
