ID A0A1H2X6C3_9BACL Unreviewed; 369 AA.
AC A0A1H2X6C3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Zn-dependent protease (Includes SpoIVFB) {ECO:0000313|EMBL:SDW88440.1};
GN ORFNames=SAMN05444487_107102 {ECO:0000313|EMBL:SDW88440.1};
OS Marininema mesophilum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Marininema.
OX NCBI_TaxID=1048340 {ECO:0000313|EMBL:SDW88440.1, ECO:0000313|Proteomes:UP000198534};
RN [1] {ECO:0000313|EMBL:SDW88440.1, ECO:0000313|Proteomes:UP000198534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45610 {ECO:0000313|EMBL:SDW88440.1,
RC ECO:0000313|Proteomes:UP000198534};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNNQ01000007; SDW88440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2X6C3; -.
DR STRING; 1048340.SAMN05444487_107102; -.
DR OrthoDB; 9781963at2; -.
DR Proteomes; UP000198534; 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; cd06160; S2P-M50_like_2; 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 Hydrolase {ECO:0000313|EMBL:SDW88440.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:SDW88440.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198534};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..136
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 141..175
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 369 AA; 40809 MW; 730B53CB5A9B7885 CRC64;
METHPRKEKH EGAWSKIGGW ATVAFGAVKF LPGLLKLGKA GGTLISMLIT IGAYALVFPW
SFSIGLVAMI FIHEMGHIWA ARHKKLPVSA PAFIPFLGAL ITLKKLPQDA ETEAYVALGG
PLVGSAGAFV CYLLGVWTGW EVLSAIAAIG FIINLFNLLP IHPLDGGRIV TAISRWFWAI
GLVGGLALII YTKSLLLIVI WLLFAFELWE AFFSRRRGKL KKVTMVAEAD VSQFLDRGLP
IPAGKDRRDL PFQQYCSMDD QEHWCDIYYP GIGIIHRMNG FSGFFEGVSL TKTDVKKGSN
GDEMLKMSLE AQYMPGDDET MLRKDKAYYQ VAPRVRLAYG TAYLGLATFL VYMLYKLGTL
PLMDSSVVS
//
