ID A0A0U2ZLE5_9ALTE Unreviewed; 1048 AA.
AC A0A0U2ZLE5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:ALS99148.1};
GN ORFNames=AT746_13365 {ECO:0000313|EMBL:ALS99148.1};
OS Lacimicrobium alkaliphilum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Lacimicrobium.
OX NCBI_TaxID=1526571 {ECO:0000313|EMBL:ALS99148.1, ECO:0000313|Proteomes:UP000068447};
RN [1] {ECO:0000313|EMBL:ALS99148.1, ECO:0000313|Proteomes:UP000068447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YelD216 {ECO:0000313|EMBL:ALS99148.1,
RC ECO:0000313|Proteomes:UP000068447};
RA Kim S.-G., Lee Y.-J.;
RT "Complete genome of Lacimicrobium alkaliphilum KCTC 32984.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP013650; ALS99148.1; -; Genomic_DNA.
DR RefSeq; WP_062481098.1; NZ_CP013650.1.
DR AlphaFoldDB; A0A0U2ZLE5; -.
DR STRING; 1526571.AT746_13365; -.
DR KEGG; lal:AT746_13365; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000068447; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04818; PA_subtilisin_1; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000068447};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1048
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006835494"
FT DOMAIN 56..156
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 184..662
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 445..528
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 718..824
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 270
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 608
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1048 AA; 108800 MW; C94C497BCD624C5F CRC64;
MTFKKSLLGS LISATLATGM IAGNSLALEV SVDRSKLQAT QSPASPSNKA KSQSASYIVQ
LKGKSGVGHA QDIGELRSSN HLAANKGNLY NAKSAKMQAY VQAMKNKQQA IAQEIGAVDV
LYNYTHTFNG FAAKLSQEQA EKLRNHPDVM GVWADEAQPL NTANTPEFLG LNGANGQHTL
GIKGDDVVVG VLDTGIWPEH PSFADDGSYS DPADIGWTGT CDAGVEADAG TFNCNNKLIG
ARYFKAGFEA TYEIQYGLGE FESPRDADGH GSHTASTAAG NEDVSASISG FPVDTVTGIA
PKARVAAYKV CWNSDYVSPE GVNERGCFYS DSMAAIDQAI EDGVDVLNYS IGGSLTDLTT
PAASAMLRAA NAGVFVSVSA GNDGPDAVTV GTPAPWVTSV GASTYDGTSA IIGNTLAVNS
GDLAGSDFLS VPAAIAPAVP EGGLSGDLVI AEPLEACGEL SNAAEMDGKI ALISRGSCAF
TDKFNNAEAA GAVGVVVYNN QAGTPFAMGG SEVNIPGAMV SNSDGVALSS SVSNSVTNIT
LTDSLIAGEA TEVGNMMAGF SSRGPNGSTE DIIKPDITAP GVRILAATTA EPMFGASGES
FAYLQGTSMS SPHIAGMAAL LKGQHPDWTP AQIKSALMTT ARQNITKEDG VTQADPFDYG
AGHAAPVNAM EPGLTYELNA GDYFAFMCGL GEGDFVTSEA GVSCSDLTGA GFSDDATQLN
YPSIAVSDLI QSKTISRTVT DMSGLGGTYV ASIDMPEGID VTVTTYDGAG NETPTDDLVV
AADGKASFAL TFNRTPDAVV NEWAFGAITW TDGNGHEVRS PIAIKAVPEV KIDVPESLSL
QLNRGRASFP VQMLYSGATS TDHAGLVAPF GSAGTVAQDP DSTYAFNEPG LGFHAYLVPE
GTQVARFSLR DSLVDAEGAD LDLYVYRCDE WSCTQVGESF NAGSNEDVIL TNPEPRANGA
IGDVYITFVH GWDLAGETTT DYTMPVWIAD QADSSTRVLS SRRAIEGRYN NITVTARGLD
PEGLYMGAIT FYDDEGVAQG TTVLEVQP
//
