ID Q89VL1_BRADU Unreviewed; 343 AA.
AC Q89VL1;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN OrderedLocusNames=blr1034 {ECO:0000313|EMBL:BAC46299.1};
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC46299.1, ECO:0000313|Proteomes:UP000002526};
RN [1] {ECO:0000313|Proteomes:UP000002526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC {ECO:0000313|Proteomes:UP000002526};
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
CC -!- FUNCTION: Extracellular zinc metalloprotease.
CC {ECO:0000256|RuleBase:RU366073}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU366073};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366073}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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DR EMBL; BA000040; BAC46299.1; -; Genomic_DNA.
DR RefSeq; NP_767674.1; NC_004463.1.
DR RefSeq; WP_011083854.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89VL1; -.
DR STRING; 224911.AAV28_02015; -.
DR EnsemblBacteria; BAC46299; BAC46299; BAC46299.
DR GeneID; 64020897; -.
DR KEGG; bja:blr1034; -.
DR PATRIC; fig|224911.44.peg.425; -.
DR eggNOG; COG3227; Bacteria.
DR HOGENOM; CLU_008590_0_1_5; -.
DR InParanoid; Q89VL1; -.
DR OrthoDB; 5378341at2; -.
DR PhylomeDB; Q89VL1; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR PANTHER; PTHR43579; -; 1.
DR PANTHER; PTHR43579:SF1; NEUTRAL METALLOPROTEINASE; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW Metalloprotease {ECO:0000256|RuleBase:RU366073,
KW ECO:0000313|EMBL:BAC46299.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Reference proteome {ECO:0000313|Proteomes:UP000002526};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT DOMAIN 103..177
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 181..342
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 170
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 265
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 343 AA; 37290 MW; C7103BC9A86DD63F CRC64;
MPCSCCIIPN DVLTRLSQDK KLSAVLRKQM VDTVQVSHEL RELRTQTAKL TSVVAARAAG
LVTLAAAPTV TVYDCKHTQT LPGTPVPKPK TSSDGSVKRT FNQTTKVARF YQQVFNRNSI
DDHGMTMMSS VHFGEKYNNA MWNGSQMVYG DGDGSIFVDF TRGNDVIGHE LTHGVTQHSL
QLAYSGDAGG LNESISDCFG SMFRQWEAKQ DVKKADWLIG RDIMGPAAKK KGFACLRDMA
DPAAKHCLAP QPTKYSQVTP GMDPHYASGP PNLAFYTACT TLGGYSWARI GQVWYHSLTG
FGPAPNMTMK AFAARTRQGA HTLYPGDAAV LAAVDTGWKK VGL
//