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Database: UniProt
Entry: Q488L4_COLP3
LinkDB: Q488L4_COLP3
Original site: Q488L4_COLP3 
ID   Q488L4_COLP3            Unreviewed;       789 AA.
AC   Q488L4;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   SubName: Full=Cold-active alkaline serine protease {ECO:0000313|EMBL:AAZ24841.1};
DE            EC=3.4.21.62 {ECO:0000313|EMBL:AAZ24841.1};
GN   OrderedLocusNames=CPS_0751 {ECO:0000313|EMBL:AAZ24841.1};
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ24841.1, ECO:0000313|Proteomes:UP000000547};
RN   [1] {ECO:0000313|EMBL:AAZ24841.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H {ECO:0000313|EMBL:AAZ24841.1};
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; CP000083; AAZ24841.1; -; Genomic_DNA.
DR   RefSeq; WP_011041600.1; NC_003910.7.
DR   AlphaFoldDB; Q488L4; -.
DR   SMR; Q488L4; -.
DR   STRING; 167879.CPS_0751; -.
DR   KEGG; cps:CPS_0751; -.
DR   HOGENOM; CLU_011263_15_3_6; -.
DR   Proteomes; UP000000547; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04817; PA_VapT_like; 1.
DR   CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR   Gene3D; 2.60.120.380; -; 2.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007280; Peptidase_C_arc/bac.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF04151; PPC; 2.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..789
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004234383"
FT   DOMAIN          163..554
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          399..481
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          599..663
FT                   /note="Peptidase C-terminal archaeal/bacterial"
FT                   /evidence="ECO:0000259|Pfam:PF04151"
FT   DOMAIN          706..774
FT                   /note="Peptidase C-terminal archaeal/bacterial"
FT                   /evidence="ECO:0000259|Pfam:PF04151"
FT   ACT_SITE        170
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        203
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        506
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   789 AA;  81945 MW;  45F282F76EECF4CC CRC64;
     MKNNRKLVLS TIALSVLAVT SAASNATPQA QLNKAEKMTT AQSSTLSFAQ WRAQQKLERT
     DYTDRLIITF KDKKQGKSVP PGLAKKIGLN LKHVKILKNN SHVIALDEMH AVKDVEKFIE
     KLRKHPSVVS IEPDYQRFLM AQNQPWGISK TQSDQLTDND AANMTVCIID SGYQRNNPDL
     NANNAAGTNN SGTGNWYENG GSHGTHVAGT IAGVNNSEGV VGILPSTNVN LHIVKVFNEA
     GWGYSGDLSD AVDTCVNNGA KVINMSLGGS GSSNTEKNAL QAAADTGVLL IAASGNDGNA
     TLSYPASYDA VMAVGALDSN NQHAEFSQYT SQVEVSAPGE AILSTVAGDG RLGFITVGST
     TYGNDSVVPQ THYIQSAGNF VVSNVDGAAN GVLSSCTISG SSYSCSNVNG NICLAERNDN
     QKGSNYPEIN PAKACADAGA SAVIVYSDST RPGLQNPFLV DANTDVTVPT VSVSRALGQQ
     LMTQLGSNAS LTVNSSQDYA YYNGTSMATP HVTGVAALVW SNNPNCTADD VRSALKNTAV
     DLDAAGRDDK TGFGLVQAKA ASDALAASCG GGTTPPPPTG NTLTNGVAKT NLGSSTELSF
     TMEVPAGATE LNFAMAGGTG DADLYVKFGS APTTSSYDCR PYKGGNTESC PIASVQAGTY
     HVKMIAYSAF TGVSLTGSFT EPTTGGGATG GSASVTDISV ARQAWTYYTI DVPAGMATLD
     FAMSGGTGDA DMYIRRGSQP TSSTYDCRPY KSGNTEACAF TNPAADTWHI GVYGYSAASG
     VSLDVTYNP
//
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