ID A0A1B7W1T1_APHFL Unreviewed; 366 AA.
AC A0A1B7W1T1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, 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=AN481_00855 {ECO:0000313|EMBL:OBQ27246.1};
OS Aphanizomenon flos-aquae LD13.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Aphanizomenon.
OX NCBI_TaxID=1710894 {ECO:0000313|EMBL:OBQ27246.1, ECO:0000313|Proteomes:UP000092382};
RN [1] {ECO:0000313|EMBL:OBQ27246.1, ECO:0000313|Proteomes:UP000092382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDT13 {ECO:0000313|EMBL:OBQ27246.1};
RA Driscoll C.;
RT "Whole genome shotgun sequence assembly of Aphanizomenon flos-aquae
RT UKL13.";
RL Submitted (SEP-2015) 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:OBQ27246.1}.
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DR EMBL; LJOY01000002; OBQ27246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7W1T1; -.
DR PATRIC; fig|1710894.3.peg.3531; -.
DR Proteomes; UP000092382; 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; 2.
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.
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:OBQ27246.1};
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 92..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 330..348
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 128..159
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 366 AA; 39521 MW; 3DCB235BDBAE4EE6 CRC64;
MSVLAAIAVL AILILVHELG HFIAARSQGI YANRFSLGFG PILLKYQGSE TEYTIRAFPL
GGFVGFPDDD PDSEIPPNDP NLLRNRPVLD RAIVISAGVI ANLIFAYLML ALQLGIVGIP
QEFQYQPGVL VKPVNEQSVA YQAGIREGDI ILAINGQEVP LGKDATTLLT KEIQTHPNQE
IDLKIQHETQ QTNLKLTPKP GADGKGIVGV ELVPNGKAIY RRPQNIIEIF KVAANRFEEL
VIGTFQGFGQ LITNFGKTVG QVSGPVKIVQ IGAQLAASDS TNLFSFAAII SINLAIINIL
PLPALDGGQL AFLLIEGLFG KPLPNKIQEG VMQTGLVLLL GLGIFLIVKE TSQLTSQLEW
VQKLLQ
//
