ID N1MKV5_9SPHN Unreviewed; 377 AA.
AC N1MKV5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=EBBID32_19120 {ECO:0000313|EMBL:CCW17571.1};
OS Sphingobium indicum BiD32.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW17571.1, ECO:0000313|Proteomes:UP000013201};
RN [1] {ECO:0000313|EMBL:CCW17571.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW17571.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Le V.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW17571.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW17571.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Nielsen J.L., Zhou N.A., Kjeldal H.;
RT "Bisphenol A degrading Sphingobium sp. strain BiD32.";
RL Submitted (APR-2013) 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}.
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:CCW17571.1}.
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DR EMBL; CAVK010000085; CCW17571.1; -; Genomic_DNA.
DR RefSeq; WP_006954705.1; NZ_CAVK010000085.1.
DR AlphaFoldDB; N1MKV5; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000013201; 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; 1.
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:CCW17571.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013201};
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 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 110..134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 295..314
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 342..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 119..198
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 377 AA; 40362 MW; E11190C9CFA16362 CRC64;
MIQNPGFVLT LLAFVAVIGP LVFVHELGHY LVGRWCGVKA EAFSIGFGPE LFAWVDKRGT
RWRVAALPLG GYVRFKGDMN AASMTDPAWL ELPAAERAQS FPSKPLWQRA AIVAAGPAIN
FLFAILILAT FAFVHGESRT PAVAGQVQPG SAAAASGILP GDRIVSLGGR EMATFDDIRL
YAQIRPGETV AMVIERDGKI FAKDGKIGSV TEDDGFGNKF QIGRLGLAPG DPVIEPVSLL
RAPVVAVERT GQIVRTMVET MGQIISGGRS VKELGGPLKI AQVSGQAATL GLESFIFFAA
LISINLGFIN LLPIPMLDGG HLLFYGIEAV QRRPVSERVQ EWAYRSGLAV LLTMMVLVTF
NDLSSFGLWK SLSGLIG
//
