ID Q1GN98_SPHAL Unreviewed; 467 AA.
AC Q1GN98;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Peptidase M48, Ste24p {ECO:0000313|EMBL:ABF54874.1};
GN OrderedLocusNames=Sala_3171 {ECO:0000313|EMBL:ABF54874.1};
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF54874.1, ECO:0000313|Proteomes:UP000006578};
RN [1] {ECO:0000313|EMBL:ABF54874.1, ECO:0000313|Proteomes:UP000006578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256
RC {ECO:0000313|Proteomes:UP000006578};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
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DR EMBL; CP000356; ABF54874.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1GN98; -.
DR STRING; 317655.Sala_3171; -.
DR KEGG; sal:Sala_3171; -.
DR eggNOG; COG4783; Bacteria.
DR HOGENOM; CLU_030556_2_0_5; -.
DR OrthoDB; 9814887at2; -.
DR Proteomes; UP000006578; Chromosome.
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; cd07324; M48C_Oma1-like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF13432; TPR_16; 2.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006578};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 51..238
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 467 AA; 50451 MW; 57855E0AA7EE1262 CRC64;
MTAFPPQPAS GAHGLRSLFH ILLTLLAMVA IAVRPAAAQS ILRDAETEAL FQDMMDPLLV
AAGLQPGQVR VHLLGDRSIN AFVAGSQDIY VFSGLIEAAD SAEEVQGVLA HELGHVMGGH
AIRINDGVSA ATSISLLSLL LGAAAIAAGG GEAGMGIMMA GQQAALGKFL AFSRVQESTA
DAAGAQYLSK AGISGRGSLA FFKKLQNLEF RYGIKQDDDQ AYGRTHPMSG DRIQALREVY
VIDPAWNKPA DPAIEKRFQR IKAKLLGYMA EPERTLRKFP ESDRSVPARY ARAYAWHKSA
YPQKALAEVE ALLEADPDDP YFLELEGQIL LESGRPDEAI PPLRQAVAKS RSQPLIAATL
GHALIATEEP AHYAEAEKVL KTAVALDNQN PFAWYQLGIV YANKGDQARA ALASAERYSL
EGRQPALALR NAEMAMQGLP QGSPDWIRAQ DISLVARAEV ERERKRR
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