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Database: UniProt
Entry: A0A098TLT8_9CYAN
LinkDB: A0A098TLT8_9CYAN
Original site: A0A098TLT8_9CYAN 
ID   A0A098TLT8_9CYAN        Unreviewed;       667 AA.
AC   A0A098TLT8;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Peptidase M48 {ECO:0000313|EMBL:KGF73274.1};
GN   ORFNames=DO97_00815 {ECO:0000313|EMBL:KGF73274.1};
OS   Neosynechococcus sphagnicola sy1.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales;
OC   Neosynechococcaceae; Neosynechococcus.
OX   NCBI_TaxID=1497020 {ECO:0000313|EMBL:KGF73274.1, ECO:0000313|Proteomes:UP000030170};
RN   [1] {ECO:0000313|EMBL:KGF73274.1, ECO:0000313|Proteomes:UP000030170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAUP A 1101 {ECO:0000313|EMBL:KGF73274.1,
RC   ECO:0000313|Proteomes:UP000030170};
RA   Dvorak P., Casamatta D., Hasler P., Poulickova A., Ondrej V., Sanges R.;
RT   "Evolution of Synechococcus.";
RL   Mol. Ecol. 0:0-0(2014).
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   -!- 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:KGF73274.1}.
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DR   EMBL; JJML01000010; KGF73274.1; -; Genomic_DNA.
DR   RefSeq; WP_036531731.1; NZ_JJML01000010.1.
DR   AlphaFoldDB; A0A098TLT8; -.
DR   STRING; 1497020.DO97_00815; -.
DR   OrthoDB; 15218at2; -.
DR   Proteomes; UP000030170; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR   PANTHER; PTHR43221:SF1; PROTEASE HTPX; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030170};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        121..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        314..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        477..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        505..526
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        647..666
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          214..442
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   667 AA;  73378 MW;  96B6A1EB10B87F4C CRC64;
     MSSPELLQAG LQALQQQRYA EAIEHLERCC QSFPHPQSSD YVPAHIALVQ AYQRSGQVER
     AIAQCQALSD SPNLQLQTWV QQALRSLKTM RQPLPSTPVS PQRRRAAAGV KLVMAQFAGN
     LALASGVTIS LLVGMVLVLC LGLLLIVDSQ QPLMGFAIAL GIVIPFNLGL FLLSPLLMDL
     TQHWLYGTRW VTLAEIESQS PAAAAVLRQV CAQRRLQQPR LGIIEDQNPT AFTYGSFPNQ
     ARLVVSQGLF TYLDADEVAT VYAHELGHIV HWDFAVMTLA ATMVQITYLI YVLAREFSDA
     GDSKIKGGLQ TGAIAAYLFY WVGTYLVLYL SRTREYYADH FAAETTGNPN GLSRALVKIA
     YGILEEGQRA DKPSKLIEGT RTLGIYDPRA AVMTGTAYRL TSDMEKMGRV FLWDMFNPWG
     WWMELQSTHP LTGKRIRALS NYAEQLGLVV EFDLARVVRE GRSLSKQKLY RNFGLDLVIY
     MGDLLGLGVG LLLGGLAVAS GAASWLVLIS LALIGFGLGT LIKTVIMFPD FQRAPTTDIL
     TLMSDPYASP LRGQPVKLEG ELIGRGDAGY VFGSDLKLQD ATGMIFLRYS SRFGGLGNFL
     FGATQVKAMI GSQVGMTGWF RRGLAPWIDL IHLQQSQGKM VESYHRFWLV VLGAGALILG
     FILPLMG
//
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