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Database: UniProt
Entry: A8LF44_FRASN
LinkDB: A8LF44_FRASN
Original site: A8LF44_FRASN 
ID   A8LF44_FRASN            Unreviewed;       393 AA.
AC   A8LF44;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Peptidase S1 and S6 chymotrypsin/Hap {ECO:0000313|EMBL:ABW09789.1};
GN   ORFNames=Franean1_0323 {ECO:0000313|EMBL:ABW09789.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09789.1};
RN   [1] {ECO:0000313|EMBL:ABW09789.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW09789.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA   Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT   "Complete sequence of Frankia sp. EAN1pec.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP000820; ABW09789.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8LF44; -.
DR   STRING; 298653.Franean1_0323; -.
DR   MEROPS; S01.513; -.
DR   KEGG; fre:Franean1_0323; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_043139_0_0_11; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0009403; P:toxin biosynthetic process; IEA:InterPro.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR003825; Colicin-V_CvpA.
DR   InterPro; IPR047680; MarP-like.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   NCBIfam; NF033740; MarP_fam_protase; 1.
DR   PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR   PANTHER; PTHR43019:SF36; SERINE PROTEASE RV3671C; 1.
DR   Pfam; PF02674; Colicin_V; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        59..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   393 AA;  40813 MW;  96536E88B8CDD3AA CRC64;
     MNLLDLVLIV LVVMFAVSGY RQGFAVGALS FVGFLGGGVL GAKVARPFAE LIGREEDGAL
     VGLIVVVGLA LVGQIAGTAL GAALRGRLTW RPGQRLDAVA GAVLSGMSVL LVAWLVATAV
     DRSPFQTLAR AARGSEVLGT VDTTMPDDVR HTFADLRRLM DDQGFPEVFA GLDGERIVAT
     DPPDPAVVSA ADVQNAAASI LKVRGQAPSC GKQVEGTGFV IAPQRVMTNA HVVAGVTEAV
     VELDSGSLPA EVVLFDPDRD VAVLHVPGLL RPPLRFQSAP PGDMGDSAVV AGYPQDGPYT
     TVPARIRNEQ VARAPDIYSR GTVRREIYAI RGRVRPGNSG GPLLSSAGTV YGVVFAAATD
     DNDTGYVLTA DEVSEPARQG AQALVPVSTQ SCD
//
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