ID I4AP21_BERLS Unreviewed; 411 AA.
AC I4AP21;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Zn-dependent protease with chaperone function {ECO:0000313|EMBL:AFM05706.1};
GN OrderedLocusNames=Fleli_3382 {ECO:0000313|EMBL:AFM05706.1};
OS Bernardetia litoralis (strain ATCC 23117 / DSM 6794 / NBRC 15988 / NCIMB
OS 1366 / Fx l1 / Sio-4) (Flexibacter litoralis).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Bernardetiaceae;
OC Bernardetia.
OX NCBI_TaxID=880071 {ECO:0000313|EMBL:AFM05706.1, ECO:0000313|Proteomes:UP000006054};
RN [1] {ECO:0000313|Proteomes:UP000006054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23117 / DSM 6794 / NBRC 15988 / NCIMB 1366 / Sio-4
RC {ECO:0000313|Proteomes:UP000006054};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Lang E., Kopitz M., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Flexibacter litoralis DSM 6794.";
RL Submitted (JUN-2012) 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}.
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DR EMBL; CP003345; AFM05706.1; -; Genomic_DNA.
DR RefSeq; WP_014799133.1; NC_018018.1.
DR AlphaFoldDB; I4AP21; -.
DR STRING; 880071.Fleli_3382; -.
DR KEGG; fli:Fleli_3382; -.
DR PATRIC; fig|880071.3.peg.3387; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_025947_3_3_10; -.
DR OrthoDB; 9781930at2; -.
DR Proteomes; UP000006054; Chromosome.
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; IPR036259; MFS_trans_sf.
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.
DR SUPFAM; SSF103473; MFS general substrate transporter; 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 Reference proteome {ECO:0000313|Proteomes:UP000006054};
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 64..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..127
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..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..203
FT /note="CAAX prenyl protease 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16491"
FT DOMAIN 206..408
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 411 AA; 46779 MW; 5FEA73D4EF914D22 CRC64;
MNASQILILI IAILVGDFLL ENFLEWLNSK KQPAHLPNHF ADIYTEDEYQ KAKSYKKANA
NFSLISNSVS FILTLVFLIT GTFGYLSDIL EVYFQSPIWH ALAFFGVVTI ASSILGLPFS
IYQTFVIEEK FGFNKTTKRL FFTDKIKGLL LGAVVGGIIG YLLLYLVLEI GQNFWIYFWI
IITIFSVGMQ FFYASLIMPL FNKLTPLEDG ELRESIEEYA GSVYFPLQNI FVIDGSKRST
KANAFFMGFG KQKKVVFYDT ILEKHTTEEL VAIFAHEVGH YKKNHIPQTM AMSIAQTGFT
LFILSQIIFS KEISLALGAT EWQIHLNMIA FGFLYSPIST VTSILFNIFS RKNEYEADNY
AKQTYGSKPL AKALKKLSAD SLSNLTPHPW YVFFNYSHPP LSERLKAMGE K
//
