ID A0A1Z4RUI0_9CHRO Unreviewed; 498 AA.
AC A0A1Z4RUI0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Peptidase M50 domain-containing protein {ECO:0000259|Pfam:PF02163};
GN ORFNames=NIES4102_31480 {ECO:0000313|EMBL:BAZ46119.1};
OS Chondrocystis sp. NIES-4102.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Chondrocystis.
OX NCBI_TaxID=2005460 {ECO:0000313|EMBL:BAZ46119.1, ECO:0000313|Proteomes:UP000217698};
RN [1] {ECO:0000313|EMBL:BAZ46119.1, ECO:0000313|Proteomes:UP000217698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4102 {ECO:0000313|EMBL:BAZ46119.1,
RC ECO:0000313|Proteomes:UP000217698};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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; AP018281; BAZ46119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4RUI0; -.
DR KEGG; chon:NIES4102_31480; -.
DR OrthoDB; 494312at2; -.
DR Proteomes; UP000217698; Chromosome.
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:SF5; ZINC METALLOPROTEASE EGY2, 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:UP000217698};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 258..429
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 498 AA; 54643 MW; 40BCDD8BA3B4725C CRC64;
MLNESQSLAT FILLAAVVLI LTWGYKRAKP YGKLGILAWL QSIVLMSPWI LFFGLFAFGL
YLNLVGILFL LVASIGVYIW LGKQLRAAGQ ESLLQQKAAA RIIRETEQSQ ESAINAKLDN
PTSPELSPIP QADLAEIKGI FGIDTFFATE TIPYQDGAIF KGNLRGDADL TYSKMNQKLE
SIFQDKYRLF LVESPEAKPV VVILPKTNDP ETTTLAQKNL ALVLFLATIL TTLEAACLLQ
GFDLFSDFGR YREAIPLSLG LWIILLAHEI GHRLLAQRYQ IRLSVPFFLP SWQIGSFGAI
TRFESLLPNR TALFDISFGG IATAGVMSFI LLVTGLTLSH PGSMYQLPTE FFRASILVGT
LAKVILGSAL EKAVVDIHPL VIVGWLGLVI TALNLMPAGK LDGGRIVHAI YGRKTARRST
VATLIILGII ALFNPNNPIP LYWAVLILFL QRDLERPVQN ELTEPDDSRA AWGLLALFLM
LATLIPLSAG LAGRIGLG
//
