ID A0A1B6YNI1_9RHOB Unreviewed; 447 AA.
AC A0A1B6YNI1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=A8B83_13080 {ECO:0000313|EMBL:OAN70424.1};
OS Rhodobacteraceae bacterium EhC02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1849170 {ECO:0000313|EMBL:OAN70424.1, ECO:0000313|Proteomes:UP000078223};
RN [1] {ECO:0000313|EMBL:OAN70424.1, ECO:0000313|Proteomes:UP000078223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC02 {ECO:0000313|EMBL:OAN70424.1,
RC ECO:0000313|Proteomes:UP000078223};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-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}.
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:OAN70424.1}.
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DR EMBL; LXYH01000016; OAN70424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6YNI1; -.
DR STRING; 1849170.A8B83_13080; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000078223; 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; 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; 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:OAN70424.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078223};
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 114..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 376..408
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 420..441
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 206..276
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 447 AA; 47211 MW; 1075BB4DC672913E CRC64;
MDIVSFLPQF GGLAMTLAAF VVALSVIVAV HEYGHYIVGR WSGIHADVFS LGFGPVLFSG
VDKRGTKWQV ALLPLGGYVK FRGDADAASA GTDGQAIRAM TEAEKRSTMH GAPLWARTAT
VAAGPIFNFV LAIIVFTAIG MTRGVAVDPL TVGELRPVAV AHEVQPGDVI LAIDGRALPQ
AGEAGFADLT AALPAVPLMD YTVLRDGREV TVQGPHPMPP VITQLAPQSA AMATDLEPDD
VILAVDGDPI FAFRQLREKV EGTEGAPLLL DVRRGDQTLQ VSLTPRRVDE PQDGGGFETN
WRIGIIGGLF FDPMTETPGF MDAFTNGVAS MWEIIRGSLS GLYHMVTGAI STCNMSGPIG
IAEVSGAMAS QGTESFIYFI AVLSTAVGLL NLFPIPVLDG GHLVFYAYEA VAGKPPSDKV
LRVLMAAGLT IILSLMVFAL SNDIFCP
//
