ID F6AJP1_PSEF1 Unreviewed; 628 AA.
AC F6AJP1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Peptidase M48 Ste24p {ECO:0000313|EMBL:AEF22910.1};
GN OrderedLocusNames=Psefu_2946 {ECO:0000313|EMBL:AEF22910.1};
OS Pseudomonas fulva (strain 12-X).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF22910.1, ECO:0000313|Proteomes:UP000000686};
RN [1] {ECO:0000313|EMBL:AEF22910.1, ECO:0000313|Proteomes:UP000000686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA Woyke T.;
RT "Complete sequence of Pseudomonas fulva 12-X.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002727; AEF22910.1; -; Genomic_DNA.
DR RefSeq; WP_013792037.1; NC_015556.1.
DR AlphaFoldDB; F6AJP1; -.
DR STRING; 743720.Psefu_2946; -.
DR KEGG; pfv:Psefu_2946; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_024494_0_0_6; -.
DR OrthoDB; 15218at2; -.
DR Proteomes; UP000000686; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd07340; M48B_Htpx_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR PANTHER; PTHR43221:SF2; PROTEASE HTPX HOMOLOG; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR PRINTS; PR00173; EDTRNSPORT.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000686};
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 17..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 105..327
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 628 AA; 67878 MW; 69222120E4B7A2F1 CRC64;
MDFFEHQDRA RRNTSRLVIL LILAVVTLVV STTLVIAIAW QVYQYGNYGL QSLSHELLLG
VAAVVVGVVL LGWAFKASQL SAGGKVVAER LGGRLLNLKP EGLHEQRVLN VVEEMALAAG
VPVPPVYLLE EPAINAFAAG LRPENAVIGI TRGAVERLNR DELQGVIAHE FSHILHGDMR
LNTRLVAVLH GILLLGLIGE LLMRGVGHSG AARTSSRSDD KGRGNAVALV MVVGLALLVI
GYAGTFFGNL IKAAVSRQRE FLADASAVQY TRNPNGIAGA LKKLGRGSRL EASHAAEYSH
MYFGQGLALS KMMATHPPLE ERIRRIDPNW KGVVLGDEVF EAPAQPTVSQ QAATAGFSAA
AASAAIASIG DPQPLHLEEA RDSLAQIDER LRDAAHDPHG ALTILYGLLL GPDDATRQQR
MTWMQANLPP LLADRLLELA EPLQRLPAGR RLPLLELAIP ALKQLEPQDF VSLKRDIGTL
LISTGQLGFM EWALLRIVER NLGMQRPVQG RLPLAALGNE SCVLLAALAR AGNVSEQAAG
EAFQAAWSTL PFTDRPFAEQ RHAGINELND ALNRLNQMRP LQKPQLLKAM ARCIEHDGRI
SAGEAELMRA VADTLDCPMP PLLSDRQA
//
