ID G6FQC2_9CYAN Unreviewed; 496 AA.
AC G6FQC2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Peptidase M50 {ECO:0000313|EMBL:EHC18007.1};
GN ORFNames=FJSC11DRAFT_1069 {ECO:0000313|EMBL:EHC18007.1};
OS Fischerella thermalis JSC-11.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Fischerella.
OX NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC18007.1, ECO:0000313|Proteomes:UP000004344};
RN [1] {ECO:0000313|EMBL:EHC18007.1, ECO:0000313|Proteomes:UP000004344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-11 {ECO:0000313|EMBL:EHC18007.1,
RC ECO:0000313|Proteomes:UP000004344};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I.,
RA Woyke T.J.;
RT "The draft genome of Fischerella sp. JSC-11.";
RL Submitted (SEP-2011) 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:EHC18007.1}.
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DR EMBL; AGIZ01000003; EHC18007.1; -; Genomic_DNA.
DR RefSeq; WP_009455347.1; NZ_AGIZ01000003.1.
DR AlphaFoldDB; G6FQC2; -.
DR GeneID; 60765267; -.
DR PATRIC; fig|741277.3.peg.1256; -.
DR Proteomes; UP000004344; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd06160; S2P-M50_like_2; 1.
DR InterPro; IPR044838; EGY1-like.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR31412; ZINC METALLOPROTEASE EGY1; 1.
DR PANTHER; PTHR31412:SF0; ZINC METALLOPROTEASE EGY1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000004344};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 250..418
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT REGION 84..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 55571 MW; 40D7D25DB0AE75DB CRC64;
MTVWFLILLG LITYLMVQRS VARLTQTPVW LLWLVLMTPA LLWTGWTVIH GAKQPLPRSL
MIWPLVICPI LYWVLFQRGR QPQQDKPTEV QAPQTEPTTL PSPEPTPVRP IQPNEEQKLR
DCFPWSVYYI QNIEYRPQAV ICRGQLRSKP NEAYQKIKEN IETKFAGRFL VFFQEDVNGK
PFFVLVPNTL ATQGNTPRKK EQLKQFGWAL LLLLATLVTT TKVGVEIAGI ELTIRQFQSN
PSLILQGLPY ALALMFILGV HELGHYLMAT RRYKIRSTPP YFIPMPFFLG TFGAFIKMRS
PVPNRKALFD VSIAGPLAGF VVTLPLLIWG LAHSEVVSLP EEKTGLLNPD ALNPKYSILL
ALLSKLALGS QLTPQSAIDL HPVAVAACLG LIVTALNLMP VGQLDGGHIV HAMFGQRNAI
LIGQVARLLL LLLSLVQPGF FLWALILLFI PLMDEPALND VTELDNQRDV WGLFAMALLV
MIILPLPQAI ASLLQI
//