ID W0RL94_9BACT Unreviewed; 568 AA.
AC W0RL94;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Oligoendopeptidase, M3 family {ECO:0000313|EMBL:AHG91202.1};
GN ORFNames=J421_3665 {ECO:0000313|EMBL:AHG91202.1};
OS Gemmatirosa kalamazoonensis.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatirosa.
OX NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG91202.1, ECO:0000313|Proteomes:UP000019151};
RN [1] {ECO:0000313|EMBL:AHG91202.1, ECO:0000313|Proteomes:UP000019151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS708 {ECO:0000313|EMBL:AHG91202.1,
RC ECO:0000313|Proteomes:UP000019151};
RX PubMed=24699952;
RA Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA Fawaz M.N., Korlach J., Tsai Y.C.;
RT "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT Phylum.";
RL Genome Announc. 2:e00226-14(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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DR EMBL; CP007128; AHG91202.1; -; Genomic_DNA.
DR AlphaFoldDB; W0RL94; -.
DR KEGG; gba:J421_3665; -.
DR PATRIC; fig|861299.3.peg.3721; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_030403_3_0_0; -.
DR InParanoid; W0RL94; -.
DR OrthoDB; 9762795at2; -.
DR Proteomes; UP000019151; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09606; M3B_PepF; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011976; Pept_M3B_oligopep-rel.
DR NCBIfam; TIGR02289; M3_not_pepF; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF48; PUTATIVE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000019151};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 162..542
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 568 AA; 63774 MW; 8DA751F49B105D06 CRC64;
MNLPDSPAAF ADATWSDIAP YFEALAAAPL DETTVAEWLA TWSRLEELLS EAGTVAMIAY
TGDTADPAKE AAHLRFSMQI FPLVDEQQVR LAKRLLDVGY APPDLATTVR RFRTDAEIFR
EANVPLFSEL EELSAAYQKI TGGLSAEWDG QRKTIPQLQP FLKSPDRAVR ERAFRLGAGA
YLEKRDELAD LFDRMYALRT RVAENAGFGN YEDFCFAAKH RFDYTPADCR RFHDAVERTV
VPALERLSAY RKSRLGVDVL RPWDLQVDVE RGGAPLKPFD TVDDFVGGAR RVFHQVDPEL
GAQFDILADE RLLDLESRPG KAPGGYCTNL HVRGRPFIFM NAVGVPDDVS TLVHEAGHCF
HDFAMTRLPL VWQRTTGHEA AELASMSMEL LAAPSLARPV GFYDDDDARA ARIEHLVDVL
ESLAHIASVD AFQSWIYTSG RGGDAAARDA AWLEIRQRFD READWTGLEP ERIARWYRQL
HIFEIPFYYI EYGIAQLGAL QVWRRSLTDH AEAVRRYRGA LALGGTRSLP EIYEAAGARL
VFDAEGMGEL VALVEEEIDR MREAAIAR
//