ID K9QR58_NOSS7 Unreviewed; 422 AA.
AC K9QR58;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:AFY48115.1};
GN OrderedLocusNames=Nos7524_2271 {ECO:0000313|EMBL:AFY48115.1};
OS Nostoc sp. (strain ATCC 29411 / PCC 7524).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=28072 {ECO:0000313|EMBL:AFY48115.1, ECO:0000313|Proteomes:UP000010378};
RN [1] {ECO:0000313|Proteomes:UP000010378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29411 / PCC 7524 {ECO:0000313|Proteomes:UP000010378};
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}.
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DR EMBL; CP003552; AFY48115.1; -; Genomic_DNA.
DR RefSeq; WP_015138560.1; NC_019684.1.
DR AlphaFoldDB; K9QR58; -.
DR STRING; 28072.Nos7524_2271; -.
DR KEGG; nop:Nos7524_2271; -.
DR PATRIC; fig|28072.8.peg.2473; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_3_2_3; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000010378; Chromosome.
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; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000010378};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 26..169
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 179..355
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 422 AA; 47944 MW; 9758622A7AF73DB4 CRC64;
MSKQQLTHPV FPASVFRLDN GLTFIHQEIP TTPVVVADVW VKAGTFHEPE PWFGMAHFLE
HMIFKGTATL APGMFDHKIE NMGGVSNAAT SYDYANYSLT TAATYLEDTL PHLGELLLNA
AIPEDEFIRE RDVVLEEIRA SYDDSDWVGF QCLLESVYQN HPYGRSILGN EEELLQHSPE
AMRCFHRAHY QPENMTVVIA GGINQQQAWD AVNRSFANFA EPVKCPQIPR VAKPVINGIR
RQELYLPHLE QARLLIAWLV PGVEHLRAAY GLDLLSVLLA EGRTSRLVRD LREELQLVQG
ICSNFSLQRE ASLFTITAWL EPEHLETVEN LILSHLDDIQ NQGINEQELA RTRRLLCNEY
AFSTETPNQL TGMYGYYNTI AQAELSVTYP QQIRSFDTQE LQQLANQYLS PQNYAVTILK
PC
//
