ID A0A420F2E6_9ACTN Unreviewed; 416 AA.
AC A0A420F2E6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=RIP metalloprotease {ECO:0000313|EMBL:RKF27120.1};
GN ORFNames=D7I43_11610 {ECO:0000313|EMBL:RKF27120.1};
OS Micromonospora globbae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1894969 {ECO:0000313|EMBL:RKF27120.1, ECO:0000313|Proteomes:UP000285744};
RN [1] {ECO:0000313|EMBL:RKF27120.1, ECO:0000313|Proteomes:UP000285744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WPS1-2 {ECO:0000313|EMBL:RKF27120.1,
RC ECO:0000313|Proteomes:UP000285744};
RX PubMed=29458491; DOI=.1099/ijsem.0.002625;
RA Kuncharoen N., Pittayakhajonwut P., Tanasupawat S.;
RT "Micromonospora globbae sp. nov., an endophytic actinomycete isolated from
RT roots of Globba winitii C. H. Wright.";
RL Int. J. Syst. Evol. Microbiol. 68:1073-1077(2018).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKF27120.1}.
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DR EMBL; RAQQ01000007; RKF27120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420F2E6; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000285744; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:RKF27120.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:RKF27120.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..364
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 165..216
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF13180"
SQ SEQUENCE 416 AA; 44751 MW; 4690733AB0799B7B CRC64;
MAYLLGVALF ALAILVSVSL HEAGHMLTAK AFGMKVTRYF VGFGPTLWSF RRGETEYGVK
GIPLGGFCKI VGMTPQDDDV DPADEPRAMW RYPVWKRTIV MSAGSITHFA LALVTLWILA
VSAGLPNPNF PSTEAEIRQE PAVVALSDCV VPDNSVRECQ PGDAASPAAQ ANLRDGDRIT
SLNGQPIDNY GELLTALRGL TPGSTATIGY VRDGQPGQTR AVLAKTERPP LDDPEGAVTP
VAALGVGLIP STPTRVTYGP VAAFGATADF TGEMAVNTVH ALQRIPQKIP ALWQAITGGE
RDMDTPISVV GASRLGGEAV ENNAWLVFFM LFVSLNFFIG VFNLLPLLPL DGGHIAIAWF
ERARSWVYAR LRRPDPGRVD YLKLMPFTYA VILIGGAFTL LTITADVVNP ITLFSR
//