ID A0A0A0BSU2_9CELL Unreviewed; 381 AA.
AC A0A0A0BSU2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN ORFNames=N868_12600 {ECO:0000313|EMBL:KGM11000.1};
OS Cellulomonas carbonis T26.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=947969 {ECO:0000313|EMBL:KGM11000.1, ECO:0000313|Proteomes:UP000029839};
RN [1] {ECO:0000313|EMBL:KGM11000.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM11000.1,
RC ECO:0000313|Proteomes:UP000029839};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas carbonis T26.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGM11000.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM11000.1,
RC ECO:0000313|Proteomes:UP000029839};
RX PubMed=26587181;
RA Zhuang W., Zhang S., Xia X., Wang G.;
RT "Draft genome sequence of Cellulomonas carbonis T26(T) and comparative
RT analysis of six Cellulomonas genomes.";
RL Stand. Genomic Sci. 10:104-104(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR006404,
CC ECO:0000256|PIRSR:PIRSR006404-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR006404,
CC ECO:0000256|PIRSR:PIRSR006404-2};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR006404};
CC Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR006404}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|PIRNR:PIRNR006404}.
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:KGM11000.1}.
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DR EMBL; AXCY01000033; KGM11000.1; -; Genomic_DNA.
DR RefSeq; WP_043605698.1; NZ_AXCY01000033.1.
DR AlphaFoldDB; A0A0A0BSU2; -.
DR OrthoDB; 9781963at2; -.
DR Proteomes; UP000029839; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR008915; Peptidase_M50.
DR InterPro; IPR016483; UCP006404_Pept_M50_CBS.
DR PANTHER; PTHR39188; MEMBRANE-ASSOCIATED ZINC METALLOPROTEASE M50B; 1.
DR PANTHER; PTHR39188:SF3; ZINC METALLOPROTEASE SLR1821-RELATED; 1.
DR Pfam; PF02163; Peptidase_M50; 2.
DR PIRSF; PIRSF006404; UCP006404_Pept_M50_CBS; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122};
KW Cell membrane {ECO:0000256|PIRNR:PIRNR006404};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006404};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006404};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR006404,
KW ECO:0000256|PIRSR:PIRSR006404-2};
KW Metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
KW Protease {ECO:0000256|PIRNR:PIRNR006404};
KW Reference proteome {ECO:0000313|Proteomes:UP000029839};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR006404};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR006404};
KW Zinc {ECO:0000256|PIRNR:PIRNR006404, ECO:0000256|PIRSR:PIRSR006404-2}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 110..133
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 145..170
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 191..210
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 222..243
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT DOMAIN 61..133
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 145..203
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT ACT_SITE 73
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
SQ SEQUENCE 381 AA; 38598 MW; B44E125C84B3B5EB CRC64;
MQTPRDARTR GWVVGRAAGA PVVVSPGWVL AAVVLTVLFA PTVRSIAFVD EVGAYAVSAV
FVLLLLGSVF LHELAHALVA RRQGVRVEEL AVTLLGGHTR LGGSAPTPRA SALVAASGPL
VNLVLGGAAW LAAELLAPTS RGSVVWLLLV AAALANGFVG LFNLVPGLPL DGGRVLEAAV
WRVTGSRSRG TAVAGWVGRA VAVLVVVWGV GRPLLAGGRP DAVGLLWTVL IGAFLWSGAG
QAVRAARADG RAARVTVRGL MRPAVAVPAR GTLLDLDTAV AHAAAPVQDA VLLAGDGRPV
AVVDAAAALS VPDERRARTA LSAVALPLPE GASVDVGLTG PDALRAVAAL ARVTPTVAVV
DGVRVVGVLR SQDVVRALRA T
//
