ID A0A1C0V165_9CYAN Unreviewed; 329 AA.
AC A0A1C0V165;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidase M48 {ECO:0000313|EMBL:OCQ91532.1};
GN ORFNames=BCR12_12000 {ECO:0000313|EMBL:OCQ91532.1};
OS Limnothrix sp. P13C2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Limnothrix.
OX NCBI_TaxID=1880902 {ECO:0000313|EMBL:OCQ91532.1, ECO:0000313|Proteomes:UP000093334};
RN [1] {ECO:0000313|EMBL:OCQ91532.1, ECO:0000313|Proteomes:UP000093334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P13C2 {ECO:0000313|EMBL:OCQ91532.1};
RA Tan B., Te S.H., Gin K., Thompson J.;
RT "Draft genome of Limnothrix sp. P13C2.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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:OCQ91532.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MBRF01000024; OCQ91532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C0V165; -.
DR STRING; 1880902.BCR12_12000; -.
DR Proteomes; UP000093334; 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 CDD; cd07325; M48_Ste24p_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR PANTHER; PTHR43221:SF3; SLL1280 PROTEIN; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000093334};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT DOMAIN 60..267
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 329 AA; 37048 MW; CC02B5F286BCE72A CRC64;
MPSYPGISSE AFRHPLDREA EQALRSLPGF DLVARKFLEV AVDRPQYLYH MGNSVQVGPR
QYASLHQLLR ECLRDLDVFP EPALFVSQSY QVNAFTIGQE QPTLVLTTAL LELLNEAELR
VVLAHELGHL KCGHSTLTQM AIWTLYAASM VGQMTMGLSN MLISNALVMA FYEWKRKAEL
SADRAALIAT DDLDTVLMTM VKVAGGSPKH LQELSLAEFK KQARDYQSLD ADAMNQAYKF
FLYNNLPQGM YSSHPFPVER ASYLQDWATS AEYQAIRRGD YQRDVAQGAV NVTANATTTA
RSPGNTEADR LRQQIEDLQR ELDRLRPAR
//
