ID Q7VD44_PROMA Unreviewed; 421 AA.
AC Q7VD44;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN Name=spoIVFB {ECO:0000313|EMBL:AAP99584.1};
GN OrderedLocusNames=Pro_0539 {ECO:0000313|EMBL:AAP99584.1};
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167539 {ECO:0000313|EMBL:AAP99584.1, ECO:0000313|Proteomes:UP000001420};
RN [1] {ECO:0000313|EMBL:AAP99584.1, ECO:0000313|Proteomes:UP000001420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120 {ECO:0000313|Proteomes:UP000001420};
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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: 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, ECO:0000256|PIRNR:PIRNR006404}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PIRNR:PIRNR006404}.
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DR EMBL; AE017126; AAP99584.1; -; Genomic_DNA.
DR RefSeq; NP_874932.1; NC_005042.1.
DR RefSeq; WP_011124693.1; NC_005042.1.
DR AlphaFoldDB; Q7VD44; -.
DR STRING; 167539.Pro_0539; -.
DR EnsemblBacteria; AAP99584; AAP99584; Pro_0539.
DR KEGG; pma:Pro_0539; -.
DR PATRIC; fig|167539.5.peg.554; -.
DR eggNOG; COG1994; Bacteria.
DR HOGENOM; CLU_037123_1_2_3; -.
DR OrthoDB; 166377at2; -.
DR Proteomes; UP000001420; Chromosome.
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 CDD; cd06164; S2P-M50_SpoIVFB_CBS; 1.
DR InterPro; IPR046342; CBS_dom_sf.
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; 1.
DR PIRSF; PIRSF006404; UCP006404_Pept_M50_CBS; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006404};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006404};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR006404};
KW Metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
KW Protease {ECO:0000256|PIRNR:PIRNR006404, ECO:0000313|EMBL:AAP99584.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001420};
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|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006404}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 46..65
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 108..130
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 192..225
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT DOMAIN 131..196
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT ACT_SITE 67
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
SQ SEQUENCE 421 AA; 46460 MW; D9062C006C6C3AB5 CRC64;
MQGVELIKLK GISLKVHPSW VFILIVFTRI SQAQFSRIFT DQFPAWQAWG VGFLTSACFF
LSVLLRELGN SFIALNEGVK VHDITLFSLG GIKRVDKQCS TPMGSLRIAI AGPLINIAIG
ILCLSCAQIV DSSNLIFLNL LSQVGVINFL LALFNLLPGL PLDGGVILKS IVWHFTGSQR
KGHRAANASG RFFSLIVIFL GGLIAFAVKG GFVLGFCLIV IGWFGLSSSR SQDQIIVLQQ
ALYDLSVKDA SRKRFRVLEH NQSLKALSEL RLSSQSENGD PQLVLLCNLG RWTGYITDKL
LMDVPAEDWD QYLLSEYSQP LTDLPSISEK RPLWYAVLEL ERVKGESLLV LNPAGLPSGT
IDRVDLSEVV LKKLGFNLPR AFLDLARKNN IYPLGISLFK IVEGMIDSGL IPKSELDKVT
K
//
