ID Y638_RHILO Reviewed; 367 AA.
AC Q98MC1;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 24-JAN-2024, entry version 114.
DE RecName: Full=Putative zinc metalloprotease mll0638;
DE EC=3.4.24.-;
GN OrderedLocusNames=mll0638;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB48192.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000012; BAB48192.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q98MC1; -.
DR SMR; Q98MC1; -.
DR KEGG; mlo:mll0638; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_1_0_5; -.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00989; PDZ_metalloprotease; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR NCBIfam; TIGR00054; RIP metalloprotease RseP; 1.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..367
FT /note="Putative zinc metalloprotease mll0638"
FT /id="PRO_0000088455"
FT TRANSMEM 108..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 121..196
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 367 AA; 39923 MW; 0E77DF0CB96D5152 CRC64;
MFLGTLVPFL FVLTVVVFVH EMGHYLVGRW CGIGVRAFSI GFGPELIGFN DRHGTRWKLC
AIPLGGYVKF VGDMNATSSQ PTSEELETLT DEERKVAFHT QAIWKRAATV VAGPLFNFLL
TIVVFSVLFA SYGRYVAEPM VAEVTADSPA AKAGIQPGDR FVSVDGSKVE TFGDVQRLVS
GRAGDTITFV MLRDGKEVTV TATPQLMEQQ DALGNKVKVA VIGVVNNKEL GQPRLITYTP
VGAVAAAVEE TGHVIQRTGQ FLQRFAVGRE DKCQLGGPVK IADMAGKAAK LGFEWLVQLV
ALLSVGIGFL NLLPIPPLDG GHLLFYGVEA VIRRPVSERM MEMAYRAGLL LVLCFMGFVF
WNDLFGC
//
