ID A0A1M4TNW0_9RHOB Unreviewed; 440 AA.
AC A0A1M4TNW0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=SAMN05444339_101430 {ECO:0000313|EMBL:SHE46108.1};
OS Loktanella atrilutea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=366533 {ECO:0000313|EMBL:SHE46108.1, ECO:0000313|Proteomes:UP000183987};
RN [1] {ECO:0000313|Proteomes:UP000183987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29326 {ECO:0000313|Proteomes:UP000183987};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU362031};
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, ECO:0000256|RuleBase:RU362031}.
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DR EMBL; FQUE01000001; SHE46108.1; -; Genomic_DNA.
DR RefSeq; WP_072855533.1; NZ_FQUE01000001.1.
DR AlphaFoldDB; A0A1M4TNW0; -.
DR STRING; 366533.SAMN05444339_101430; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000183987; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362031};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362031};
KW Metal-binding {ECO:0000256|RuleBase:RU362031};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU362031};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SHE46108.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183987};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362031};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU362031}.
FT TRANSMEM 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 110..138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 415..433
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 198..268
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 440 AA; 46748 MW; 4C7ECFC3473AB995 CRC64;
MDLTQLLPQL GGGLFTLLAF VVSLSIIVAI HEYGHYIVGR WSGIHAEVFS LGFGPVIYSR
TDRRGTVWQV AALPFGGYVK FLGDANAASV GGTTTVAGHD PRNTMAGAPL WARAATVAAG
PVFNFILAVA LFAAYLMVTG MPTDPVTYKD EVALPPAYAS DLRPGDQIVK VGAVDMGGDV
SLDTLPVTDR VDYTVRRDGS DVVVQGPYPL PPRASGVTPR SAADDAGLRI GDVITAIDGQ
PIFAFRQIVD VVNAADGRSL DLTIWRDGAT RDVTLAPRRM DLPKADGTFE TRWLIGITGD
LFFQTATDTV APWTALWLGM KQLWFSITMS LSALSHMISG DISTCSLSGP VGIAETSATM
AGQGLASYMS FIAVLSAGVG LLNLFPIPIL DGGHLVFYAY EAVTRRKPSE RAMNVMMIGG
LTIIAGMMVF SILNDLLLCP
//
