ID L8M2C2_9CYAN Unreviewed; 495 AA.
AC L8M2C2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:ELS04029.1};
GN ORFNames=Xen7305DRAFT_00037570 {ECO:0000313|EMBL:ELS04029.1};
OS Xenococcus sp. PCC 7305.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC Xenococcus.
OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS04029.1, ECO:0000313|Proteomes:UP000011203};
RN [1] {ECO:0000313|EMBL:ELS04029.1, ECO:0000313|Proteomes:UP000011203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS04029.1,
RC ECO:0000313|Proteomes:UP000011203};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:ELS04029.1}.
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DR EMBL; ALVZ01000139; ELS04029.1; -; Genomic_DNA.
DR AlphaFoldDB; L8M2C2; -.
DR STRING; 102125.Xen7305DRAFT_00037570; -.
DR PATRIC; fig|102125.3.peg.1643; -.
DR eggNOG; COG0612; Bacteria.
DR Proteomes; UP000011203; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000011203}.
FT DOMAIN 43..87
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 141..237
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 245..423
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 495 AA; 56052 MW; 22ED928FCE1547CE CRC64;
MIAFVGNSNL VRANDEISLQ PYITRFLDRV TEFQLDNGMK FIVIENHDAP VVSFVTYADV
GGVDEPDGQT GVAHFLEHLA FKGTKSIGTK DYKQEKVYMD QLDRLFAQIK AAKIAGDEAK
LAQLTAEFSN IESQAGSLVK QNEYGQIVDT AGGVGLNAVT TSDYTSYFYS FPSNKLELWM
SLESERFLNP VFREFYKEKQ VILEERRMRT DNSPIGKTIE EFLDTAFTSH PYKRPTIGYN
EDIRNLTRQN VRDFFVTYYT PNNLTVAIAG DVDPQEVQEL AEVYFGRFEE RTAPPEVTKT
EPKQTETKEV IVKLPTQPWY LEGYHVAGLN DPDYPVYNLL TNILSSGRTS RLYQSLVEEQ
QVALSAQGFS GFPGNKHPNL MLFYALTAPG HTVDDVAIAL REQIELLKTE PVTTAELARI
KTQFKASLLR SLESNLEMAR ILTEYEAKTG DWRNLFNELE AITEVTADDI QRVAQNIFTD
ENRTIGKLLS VNNKQ
//
