ID D0I733_GRIHO Unreviewed; 618 AA.
AC D0I733;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Protease IV {ECO:0000313|EMBL:EEY72452.1};
GN ORFNames=VHA_001552 {ECO:0000313|EMBL:EEY72452.1};
OS Grimontia hollisae CIP 101886.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=675812 {ECO:0000313|EMBL:EEY72452.1, ECO:0000313|Proteomes:UP000003604};
RN [1] {ECO:0000313|EMBL:EEY72452.1, ECO:0000313|Proteomes:UP000003604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 101886 {ECO:0000313|EMBL:EEY72452.1,
RC ECO:0000313|Proteomes:UP000003604};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C.,
RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A.,
RA Bartels D., Vonstein V.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
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:EEY72452.1}.
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DR EMBL; ADAQ01000011; EEY72452.1; -; Genomic_DNA.
DR RefSeq; WP_005503421.1; NZ_ADAQ01000011.1.
DR AlphaFoldDB; D0I733; -.
DR GeneID; 58897086; -.
DR eggNOG; COG0616; Bacteria.
DR OrthoDB; 9764363at2; -.
DR Proteomes; UP000003604; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd07018; S49_SppA_67K_type; 1.
DR CDD; cd07023; S49_Sppa_N_C; 1.
DR Gene3D; 6.20.330.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR004634; Pept_S49_pIV.
DR InterPro; IPR004635; Pept_S49_SppA.
DR InterPro; IPR002142; Peptidase_S49.
DR InterPro; IPR047217; S49_SppA_67K_type_N.
DR InterPro; IPR047272; S49_SppA_C.
DR NCBIfam; TIGR00705; SppA_67K; 1.
DR NCBIfam; TIGR00706; SppA_dom; 1.
DR PANTHER; PTHR33209; PROTEASE 4; 1.
DR PANTHER; PTHR33209:SF1; SERINE PROTEASE SPPA, CHLOROPLASTIC; 1.
DR Pfam; PF01343; Peptidase_S49; 2.
DR PIRSF; PIRSF001217; Protease_4_SppA; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EEY72452.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003604};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..290
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 391..541
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 208
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT ACT_SITE 408
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 618 AA; 68248 MW; 6C6122B545BE8C7B CRC64;
MKTLFKFIGT FFKWCWKALS FARQLILNIL FIAILVGIYF VFTTEHETQT KPIEQPEQAL
LVDIAGPIVE KRRRIDPYDF ATRNLFGQQM HVENVLYDIV DQIRAGAKDD KINGMVLSLS
DMSETSLTKL RYIAKAINEF KATGKPVVAI GDHYNQSQYY LASYADEIFM APDGAVLLRG
YGSYNLYFKE LLENLDVTTH VFRVGTYKSF VEPYTRTDMS EEAREANSVW LNQLWAAFVD
DVATNRNIDP AVLTPDAPSL IAKLKEAGGD FAKLAQNMGL VDELLTRQQT RLRLADMLGS
DGQDSFNYVS IYDYAPLDFD YPKANQIAVV VASGAIIDGF ETEGTIGGDT TAALLRDARL
NDAIKAVVLR VDSPGGSAFA SEVIRNEVDA LKKAGKPVVV SMSSVAASGG YWISSSANRI
LAQPTTITGS IGIFGILTTF EDVLAKYGVY NDGIGTTPFA GVGVTRALPD EISDIMQLGI
ENGYQRFIGL VASERNLSLE DVDQVAQGRV WTGYDAMKRG LVDQMGDFDD AIAVAAELAK
VEEYSLNWME EPLTPAQQFI YNLISQAMVM LDVQPLITLP KTAQQFANAA ITEINNLNNF
NDPNGQYALC PNCSYYEN
//