ID A0A1Z4QV83_9CYAN Unreviewed; 609 AA.
AC A0A1Z4QV83;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Protease 4 {ECO:0000256|PIRNR:PIRNR001217};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR001217};
DE AltName: Full=Endopeptidase IV {ECO:0000256|PIRNR:PIRNR001217};
DE AltName: Full=Protease IV {ECO:0000256|PIRNR:PIRNR001217};
DE AltName: Full=Signal peptide peptidase {ECO:0000256|PIRNR:PIRNR001217};
GN ORFNames=NIES4101_89630 {ECO:0000313|EMBL:BAZ42991.1};
OS Calothrix sp. NIES-4101.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=2005461 {ECO:0000313|EMBL:BAZ42991.1, ECO:0000313|Proteomes:UP000290974};
RN [1] {ECO:0000313|EMBL:BAZ42991.1, ECO:0000313|Proteomes:UP000290974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4101 {ECO:0000313|EMBL:BAZ42991.1,
RC ECO:0000313|Proteomes:UP000290974};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|PIRNR:PIRNR001217}.
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683, ECO:0000256|PIRNR:PIRNR001217}.
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DR EMBL; AP018280; BAZ42991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4QV83; -.
DR Proteomes; UP000290974; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Cell inner membrane {ECO:0000256|PIRNR:PIRNR001217};
KW Cell membrane {ECO:0000256|PIRNR:PIRNR001217};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001217};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR001217};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001217};
KW Reference proteome {ECO:0000313|Proteomes:UP000290974};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..286
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 382..532
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 202
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT ACT_SITE 398
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 609 AA; 66671 MW; DAC0BE05C355A962 CRC64;
MRNFIKQTFA SVIGSLLGLI IFCGAGTTGL FLLLFALASS KNIGPEVKDK SVIVFDLAMN
ITDSEPSSGE VFQEALSGTS KERMSLRNVL DTIEKARKDQ RIVGIYLDAT RVSQSSSVAG
FATLKEIRQA LEEFRTTGKK IIAYGMEWGE REYYLSSIAD TVVVNPLGAM EINGFSSQPM
FLSGALQKYG VGVQVIRVGK FKGAVEPFVL NKLSNENRQQ TQALLNDVWG EWRTAVGKSR
KITPQKLQTV ADSKAFLEAN EAKQQGLIDK VAYQDQVVSD LRKLTNTTSE DKTFKQISIS
DYAQVVDKGT ENQSKNKIAI VYAEGEIVDG TGEDGQVGGD RFAKIFNKIR QDKNVKAVVL
RVNSPGGSAT AAEVMQREIQ LTREKIPVVV SMGDVAASGG YWIATDSNRI FAEPNTITGS
IGVFGLLLNF QKVANDNGIT WDAVKTGKYA DNQTVARPKS PEELAVYQRS VNRIYNLFLN
KVAQGRKLPQ TKVAEIAQGR VWSGTAAKNI GLVDEIGGLD AAIAHAAGLA NLGGNWKLQE
FPKGSSFGER FFGRAVEETQ TNLGINPSKQ QNYPLTQELQ KLQKEISVLQ NLNDPLNIYA
RLPFNLKIE
//