ID K9HRA8_9PROT Unreviewed; 592 AA.
AC K9HRA8;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Protease IV {ECO:0000313|EMBL:EKV30946.1};
GN ORFNames=C882_4283 {ECO:0000313|EMBL:EKV30946.1};
OS Caenispirillum salinarum AK4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=1238182 {ECO:0000313|EMBL:EKV30946.1, ECO:0000313|Proteomes:UP000009881};
RN [1] {ECO:0000313|EMBL:EKV30946.1, ECO:0000313|Proteomes:UP000009881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK4 {ECO:0000313|EMBL:EKV30946.1,
RC ECO:0000313|Proteomes:UP000009881};
RX PubMed=23409257;
RA Khatri I., Singh A., Korpole S., Pinnaka A.K., Subramanian S.;
RT "Draft Genome Sequence of an Alphaproteobacterium, Caenispirillum salinarum
RT AK4(T), Isolated from a Solar Saltern.";
RL Genome Announc. 1:E00199-12(2013).
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:EKV30946.1}.
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DR EMBL; ANHY01000007; EKV30946.1; -; Genomic_DNA.
DR RefSeq; WP_009540391.1; NZ_ANHY01000007.1.
DR AlphaFoldDB; K9HRA8; -.
DR STRING; 1238182.C882_4283; -.
DR PATRIC; fig|1238182.3.peg.1945; -.
DR eggNOG; COG0616; Bacteria.
DR OrthoDB; 9764363at2; -.
DR Proteomes; UP000009881; 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 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:EKV30946.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009881};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 122..271
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 372..522
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 194
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT ACT_SITE 389
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 592 AA; 63037 MW; 0E7BBB4B45DE82F6 CRC64;
MRALGKFLLG TLAVIGFLFL GLIGLAWWGI SSLDFEEMMA GGAERPDQMV LTVDLRREFP
EGEPEGPFAL LPDGAPLSLS ATVRAIDAAA ADPDVRGLLA EIGGTQAGMA QAQALRAAVA
RFRASGKPAI IFAETLNEGN DSLDTYIATA FDEVWLQPSG GVGPLGFATE VPFLRNLLEE
VGVRPQFDAR EDHKSAFDSL TRDSMDQFQR EDLQDLLGGF WSQFVTDVAA DRNLSPETVR
QVAQQSPLLA PEALDSGLVD RLAYRDEVEA EVFTRAGTQE TLPLEAYAGV ELEEAPEAAP
RVALIQASGP IMRGEAEKGP LGGGAGIYSD TLSRAIEAAV EDGGVRAIVL RIDSPGGSYV
ASDTVWRTIR RARDRGMPVV VSMGNTAASG GYFIAMAGDH IVAEPGTVTG SIGVVSGKFV
LSDLWRKLEV NWDDVSVGGP RLMYSPNQDF TQAQWAEFQK NLDWIYNDFV SKVAEARGMT
KQQVRGLAGG RIWTGAAAAE KGLVDSLGGL DEAVAEAKRR AGIATDTAVA LEPFPKPATG
LDRLLEALES TPLAGSEAEA LAALARVAAM LEPLTRRIEA MEQGPLRAPV VE
//
