ID A0A099Y3G9_9FLAO Unreviewed; 436 AA.
AC A0A099Y3G9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Peptidase, M48 family {ECO:0000313|EMBL:KGL63110.1};
GN ORFNames=PHEL85_0141 {ECO:0000313|EMBL:KGL63110.1};
OS Polaribacter sp. Hel1_85.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250005 {ECO:0000313|EMBL:KGL63110.1, ECO:0000313|Proteomes:UP000029991};
RN [1] {ECO:0000313|EMBL:KGL63110.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_85 {ECO:0000313|EMBL:KGL63110.1};
RA Xing P., Hahnke R.L., Unfried F., Markert S., Huang S., Barbeyron T.,
RA Harder J., Becher D., Schweder T., Gloenk F.O., Amann R.I., Teeling H.;
RT "Niches of two polysaccharide-degrading Polaribacter strains isolated from
RT the North Sea during a spring diatom bloom.";
RL ISME J. 0:0-0(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
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}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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:KGL63110.1}.
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DR EMBL; JPDS01000001; KGL63110.1; -; Genomic_DNA.
DR RefSeq; WP_036819781.1; NZ_JPDS01000001.1.
DR AlphaFoldDB; A0A099Y3G9; -.
DR STRING; 1250005.PHEL85_0141; -.
DR eggNOG; COG4783; Bacteria.
DR OrthoDB; 910748at2; -.
DR Proteomes; UP000029991; Unassembled WGS sequence.
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 Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..436
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001957106"
FT DOMAIN 106..314
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 436 AA; 51756 MW; 3EF56FCCE71FC14C CRC64;
MIKKITAIFV LLFSINFSAQ TLRLIDTSDF EIRKKLTKNL KKTHSLFYKS LKKEYKGKLR
IEITNLYKSK HKEFLKNVNK EKIIFDTLFT KYTDSLSKVI INSNPKLKDK NLSIYISKNP
SINALNIGDG IIFLNIGLFK YFENEDQLVS VLSHEIAHEN LNHVSDNMIR IAKLRTSKLR
KDQARRIKKE KYNTYDKSFS ILKNLLYSDS KTHRKKEMQA DSVGYLLYKN TTLYKPNYIS
ALQLLADYEK LPTINLDSTV YRRFFDIPKQ PFKDSWLKME KFSDYDYSKY TEKINKDSVK
SHPEFTERIL KLKKDFPELS INDSLSKSSK GKTFSRLQKI AKEGDIVNFY DLEEYGYSIR
LILHKLSKDS TNSYLKKWLG KNFLSLYKAK KKYQLNRYIE RINPKKQTKE YQQFLSFIWN
LNLEEIKNIG DYYTEN
//
