ID Q46GP0_PROMT Unreviewed; 396 AA.
AC Q46GP0;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN OrderedLocusNames=PMN2A_1868 {ECO:0000313|EMBL:AAZ59356.1};
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59920 {ECO:0000313|EMBL:AAZ59356.1, ECO:0000313|Proteomes:UP000002535};
RN [1] {ECO:0000313|EMBL:AAZ59356.1, ECO:0000313|Proteomes:UP000002535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A {ECO:0000313|EMBL:AAZ59356.1,
RC ECO:0000313|Proteomes:UP000002535};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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}.
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DR EMBL; CP000095; AAZ59356.1; -; Genomic_DNA.
DR AlphaFoldDB; Q46GP0; -.
DR STRING; 59920.PMN2A_1868; -.
DR KEGG; pmn:PMN2A_1868; -.
DR HOGENOM; CLU_037123_1_2_3; -.
DR PhylomeDB; Q46GP0; -.
DR Proteomes; UP000002535; 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; 2.
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 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|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR006404};
KW Metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
KW Protease {ECO:0000256|PIRNR:PIRNR006404};
KW Reference proteome {ECO:0000313|Proteomes:UP000002535};
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 34..52
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 93..114
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 134..160
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 197..214
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT DOMAIN 45..114
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 122..167
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT ACT_SITE 54
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
SQ SEQUENCE 396 AA; 44149 MW; EA31F6952D50C3B3 CRC64;
MRIHPSWFLV FLYFTLSAKD QFETLLNGQA SIWNGWVIGA STSSLLFLSV LLHELAHSFV
AIGEGLKVRD ITLFFLGGMA SLEKECPTSK GSLKIAISGP VVSLLLAFLM ILLSNNLSVS
NFILSNLFKQ VGSLNLLIGV FNLLPIMPLD GGVILKSLIW YFTGSKRAGI KVAIGSARLI
SFLAIFIGIL SLLRGNFYLS ICFSIIGLFV FSSSKSQSQI IQIQKILSEL YVNQVCSRSF
RVLEDDLPVK VLSKYSSFNK DNFSNEVWIL LCREGRWVGY VNEKILKNIS VQNWDKKFLY
EFSQPINELP SISEKESLWK AILKIEKTKD GRLLVLSFSG LPLGTLDRVD LGKAVLKKIG
LNLPDQLIKI ARKENIYPLG LNLPNIAQSM DSSDLI
//
