ID A0A251WB16_9CYAN Unreviewed; 494 AA.
AC A0A251WB16;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Site-2 protease family protein {ECO:0000313|EMBL:OUC12297.1};
GN ORFNames=B0A82_23205 {ECO:0000313|EMBL:OUC12297.1};
OS Alkalinema sp. CACIAM 70d.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Alkalinema.
OX NCBI_TaxID=1934309 {ECO:0000313|EMBL:OUC12297.1, ECO:0000313|Proteomes:UP000194922};
RN [1] {ECO:0000313|EMBL:OUC12297.1, ECO:0000313|Proteomes:UP000194922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CACIAM 70d {ECO:0000313|EMBL:OUC12297.1};
RA Lima A.R., Siqueira A.S., Pereira J.S., Goncalves E.C.;
RT "Draft genome of Alkalinema sp. CACIAM 70d.";
RL Submitted (JAN-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}.
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:OUC12297.1}.
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DR EMBL; MUGG01000191; OUC12297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251WB16; -.
DR STRING; 1934309.B0A82_23205; -.
DR Proteomes; UP000194922; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:OUC12297.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:OUC12297.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000194922};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 376..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 426..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 468..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 246..422
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 494 AA; 54860 MW; 2DE015C19D48E1DA CRC64;
MIWFFLLLGF LGLVSYAFIV KRVTSVTRTP AWLLWLVVMT PAFSLMVWTV LFGRTPMPIG
LAILLFLGCF LLYLYLIQRG RIVPDPRSAP QEVEPVQSSE PPIELPTEPV MTRPINKEEE
DHLKSCFPWS VYYLQHLEYR PQAVICRGQL RSKPEVAYQT IRENIEAHFG KRFYVVFQEG
GDRKPFFVLV PNPFAQLDFS PRALRRPKVA VILAIVTAFT TTWAGQQLLQ QVGMRGNPSF
WEGVPYAIAL MGFFAIREGG HYWTTLRYGI PATLPYFIPV LPLPQLPIGT VGAFLQIRSP
IPNRKALFDV GMFGAMVGLG VAVILLVVGL TQSQIVNATE HPSVFKFEAL LPQYSLLLTL
ACKVVFGNAL TAKSAIALNP IAVAGWLGIL FTAFNLMPVG QLDGGRMVHA VYGQRAGAMI
GQVARLLLLV LALMQPHLLL WAVLLFLLPT IDEPALNDVT ELDSTRDMIG LIALFLLIVI
ILPTPGVLLN ALGM
//
