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Database: UniProt
Entry: A0A316DZQ9_9FLAO
LinkDB: A0A316DZQ9_9FLAO
Original site: A0A316DZQ9_9FLAO 
ID   A0A316DZQ9_9FLAO        Unreviewed;       410 AA.
AC   A0A316DZQ9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=STE24 endopeptidase {ECO:0000313|EMBL:PWK22033.1};
GN   ORFNames=LX92_03385 {ECO:0000313|EMBL:PWK22033.1};
OS   Maribacter polysiphoniae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=429344 {ECO:0000313|EMBL:PWK22033.1, ECO:0000313|Proteomes:UP000245667};
RN   [1] {ECO:0000313|EMBL:PWK22033.1, ECO:0000313|Proteomes:UP000245667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23514 {ECO:0000313|EMBL:PWK22033.1,
RC   ECO:0000313|Proteomes:UP000245667};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR627057-2,
CC         ECO:0000256|RuleBase:RU003983};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR627057-2,
CC       ECO:0000256|RuleBase:RU003983};
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:PWK22033.1}.
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DR   EMBL; QGGQ01000009; PWK22033.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316DZQ9; -.
DR   OrthoDB; 9781930at2; -.
DR   Proteomes; UP000245667; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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:0071586; P:CAAX-box protein processing; IEA:InterPro.
DR   CDD; cd07343; M48A_Zmpste24p_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR027057; CAXX_Prtase_1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   InterPro; IPR032456; Peptidase_M48_N.
DR   PANTHER; PTHR10120; CAAX PRENYL PROTEASE 1; 1.
DR   PANTHER; PTHR10120:SF24; CAAX PRENYL PROTEASE 1 HOMOLOG; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
DR   Pfam; PF16491; Peptidase_M48_N; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR627057-2};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003983};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR627057-2}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        98..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        286..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        328..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..203
FT                   /note="CAAX prenyl protease 1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16491"
FT   DOMAIN          206..409
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT   ACT_SITE        358
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT   BINDING         280
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT   BINDING         354
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
SQ   SEQUENCE   410 AA;  46643 MW;  16E071E424098AAA CRC64;
     MTQTSLFYII IAILVIEFII ETTLDHLNSK RYNDPIPDDL KDVFDTEEYQ KSQEYKKTNY
     KFGLLTSTFS LLLTLGFLSL GGFEWIDTLA RSVSDNPIII ALVFFAIIMI GSDLITTPFG
     YYKTFVIEER FGFNKTSKTT FFTDKLKGYL MMAIIGGGLT ALIIWFFEWA GTNFWIYAWA
     VVAIFTLFMN LFYSRLIVPL FNKQKPLEEG SLKNKIEGYA QKVGFEIRNI FVIDGSKRST
     KANAYFSGFG KEKRVTLYDT LINDLDEDEI VAVLAHEVGH YKRHHIVFNL ISSILLTGFT
     LFLLSLFINS PEVSRAIGVS QPSFHAALIG FGILYSPISE VTGLIMNYLS RKFEYQADDF
     AKNTFAAKPL ITSLKKLSKN SLSNLTPHPA YVFMHYSHPP LIARVKNLKA
//
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