ID F2R6P4_STRVP Unreviewed; 459 AA.
AC F2R6P4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Peptidase, M16 family {ECO:0000313|EMBL:CCA58673.1};
GN OrderedLocusNames=SVEN_5387 {ECO:0000313|EMBL:CCA58673.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA58673.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA58673.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA58673.1};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; FR845719; CCA58673.1; -; Genomic_DNA.
DR RefSeq; WP_015036569.1; NZ_JABVZO010000046.1.
DR AlphaFoldDB; F2R6P4; -.
DR STRING; 953739.SVEN_5387; -.
DR GeneID; 69867454; -.
DR KEGG; sve:SVEN_5387; -.
DR PATRIC; fig|953739.5.peg.530; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_3_3_11; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000006854; 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; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000006854}.
FT DOMAIN 45..192
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 199..380
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 459 AA; 49635 MW; 8622005F98949D09 CRC64;
MTSRSSVTTA RPSSEGRAVA RTQTLLPGKD GIGTVRRTTL PGGLRIVTET LPSVRSATFG
IWAHVGSRDE TPTLGGATHY LEHLLFKGTR KRSALDISAA IDAVGGEMNA FTAKEYTCYY
ARVLDTDLPL AIDVVCDMLT DSLILEEDVD AERGVILEEI AMTEDDPGDV VHELFARTMF
GDTPLGRPVL GTVDTVNGLT RGQIARFYRK HYDPTHLVVA AAGNVDHATV VRQVRRAFEK
AGALGRTDGV PVAPRTGVRT LRAAGRVELL NRKTEQAHVV LGMPGLARND ERRWALGVLN
TALGGGMSSR LFQEVREKRG LAYSVYSYTS GFADCGLFGV YAGCRPGQVH DVLKICRDEL
HKVASDGLTD DEIARAVGQL SGSTVLGLED TGALMNRIGK SELCWGTQMS VDDMLDRIAA
VTPDEVREVA RDVLEQRPSL SVIGPLKDKQ ADRLHQAVS
//