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Database: UniProt
Entry: H3NY12_9GAMM
LinkDB: H3NY12_9GAMM
Original site: H3NY12_9GAMM 
ID   H3NY12_9GAMM            Unreviewed;      2180 AA.
AC   H3NY12;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Subtilisin-like serine protease {ECO:0000313|EMBL:EHQ56736.1};
GN   ORFNames=OMB55_00004530 {ECO:0000313|EMBL:EHQ56736.1};
OS   gamma proteobacterium HIMB55.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX   NCBI_TaxID=745014 {ECO:0000313|EMBL:EHQ56736.1, ECO:0000313|Proteomes:UP000003408};
RN   [1] {ECO:0000313|EMBL:EHQ56736.1, ECO:0000313|Proteomes:UP000003408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIMB55 {ECO:0000313|EMBL:EHQ56736.1,
RC   ECO:0000313|Proteomes:UP000003408};
RX   PubMed=22493201; DOI=10.1128/JB.00171-12;
RA   Huggett M.J., Rappe M.S.;
RT   "Genome Sequence of Strain HIMB55, a Novel Marine Gammaproteobacterium of
RT   the OM60/NOR5 Clade.";
RL   J. Bacteriol. 194:2393-2394(2012).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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:EHQ56736.1}.
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DR   EMBL; AGIF02000001; EHQ56736.1; -; Genomic_DNA.
DR   STRING; 745014.OMB55_00004530; -.
DR   PATRIC; fig|745014.4.peg.454; -.
DR   eggNOG; COG1404; Bacteria.
DR   OrthoDB; 9795680at2; -.
DR   Proteomes; UP000003408; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd14256; Dockerin_I; 1.
DR   CDD; cd00102; IPT; 1.
DR   CDD; cd07473; Peptidases_S8_Subtilisin_like; 1.
DR   Gene3D; 2.60.40.680; -; 1.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_dom.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034204; PfSUB1-like_cat_dom.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF01833; TIG; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00429; IPT; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 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};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000003408};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..2180
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003591448"
FT   DOMAIN          1580..1663
FT                   /note="IPT/TIG"
FT                   /evidence="ECO:0000259|SMART:SM00429"
FT   REGION          2083..2156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2130..2151
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        263
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        323
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        496
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   2180 AA;  234577 MW;  3291210275E5C4AF CRC64;
     MRYLKLIPVG LMIAALSYAQ EPEDVSGSET AAAKSDRVIS EPDFHVLKRQ RSFRGPYTDQ
     DDPLLLAEQS KENARTGVNP NELSCRPPHC SREDARLIIK LATPASAQAL AKATGNSSKQ
     SAYFVDTSLT PIFSQSQVTK ARAKLVSTRT KMPLNSMGKP VDLMRWRSLA LPAGTDLDEA
     IADLSLDPRV EVVESSFERQ LKGELSKPGE DSSMSTLAVV ANDPRKGEQW ALERTRTEDA
     WQWLEDNGYP AWGDRNIVVA VIDSGVDYTH EDLAGNMWVN AGEIPGNGID DDNNGFVDDV
     YGADVVGQEG QDHDGDPQDD NGHGTHVAGI IAAQGNNDIG IIGVAPNAQI MAIKAAQYSG
     VLTSTDISEA ILYAYQQGAD IINMSFGGSG RSVLEEEALA VAFSNAVLVA AAGNQGIYND
     RNCGIFARPS YPAAYPYVLG VMAESQFVAA NGDWLAGFSN WDCKARNGLE YEVMAPGVDV
     LSTIPGNGYA AWDGTSMAAP VAAGMAALVR TRFDDKSVYS SRFIMGQVAS TGASKQGNTP
     CRGCLPKSYL SADALTALTE VPEPSLSYLK HYLFDETDRA GNDGDGIVDA GETIDLALII
     KNYWGMADNV EVTLEAQAAG AVAGPDPYVT WDVPTVNYGG VGSFNEDDNG LIYDDEQYIT
     GVNSPFRFTV AADTPNEHII PMLVTMTATN GLDPNDTSTY TTTSRFNLIV QRGRELPRVI
     DSDAPGTDGG QIDTDGVEDG VVTIDDSTLW LIDNPVLIAE DTTLKVGPGA TLQFWGTQPD
     DTYAVFENPY LQVEGTLDVE GTVEKPAVFK PSDLFPDRAV VIDNRSIVRI RHAELYNLSR
     QQQVTGYQNY NFDLIDHSLV TRVALDGWLV VRRSESGYFS TNPGVTFGVS TLSNSRLNRL
     GNELPYAREI DNVVTQSTGP AQFFMGGYGW EQALVWERAE TSLFDGTYLN SSQYQYRFLP
     ELRSSVLLNN NQSWVNRYGE TVTQGSRGQL PPYALSSRSL VLTTSQIDDR TYALIVMANP
     NQQLPYSSWE SKALAFNEFA SSLGGSLLVY SSDDERDKVQ SWLAGYWNRL DTETSEQLLD
     LCGDNLAFCQ WMKGQKWDAN QFAYGVYRDE NGWGWITGEE PELTGYDPTK DANIIENSDA
     RFVLGYACCT QSYNFASPKL ALVELPSLLT QLEVQSELDE WIEARPSAVS GNAILNQWWD
     PVPNHWMVIE TPNKYDDFGL FSDSVDMTGV FWGTQSEELI RNAVRSYQTD FNKLPATIFP
     AATTPSDSAY PFVVDVDIKD SDGNARADSR FASEGTVWDV TFNRDMDASV QPMVTFGPDV
     PYTDFTVPGD WIDARTWRGE VTISPVATDG YQYVRVAGAV AADDPGLVTG NDQKRFRFEV
     ITSGTESLNL QASGGEGYVD LSWNQDDYDT LMGFNIYRST SQDGNYVRIN QTLVGNEDRE
     YRDSNTEPGV QYFYYFTVAL DGSESEPSNK ASATPIDTVK PVMSHNIIST ATFGSTVMVQ
     ANVTDNISVQ SVTLYYRAIG DTTYTSVDMV NTSGSTYRAS IPASATQPPG VEYYIAATDG
     SSYTYNGRAS SPNKITVENN PVVTSVSPSA GSTAGGEVIS VSGNNFVDGA TVALGSATCQ
     NVVWASESRL TCTTPASAPN LVAVTVENPD GGKGVLTSAF TFVGNSTTMA LPDITASQGQ
     TRDVALTVDP VSGMQSFTAV ISWNGDHLQY AGFTKGALVS GWDVVSQLEG TTLTIAGSSS
     TSVSGSGELV LLEFGVVADG DVSSVIDLVS AQINEGYIET ALVDGSFTTA AGFSISGQVR
     FWDASNTAVA ASVTLDNTLE ETSDEATGHF QFSGVLDGTH TLNIGKEDGI NDSIRGYDAS
     LILSHVVGSA TLTGSALAAA DVTGNGEISA LDASKVLEVA AGLETVPFAN QASPWTFEPA
     ERRYDEVTSN ITDADFTAIY MGDVSGNWGE LSTQSSTGVR LELDSITREG IATVNVLAAP
     PVEGTAISSV ELTLNTTAGV SLIQASRTPS TNNWSEPLVT VGDNAFSAII YDDVSGAFST
     ETHVLSLELS LTNGQQAVTS MGGWLNEMQL YSSEAFALKS ANDTDGDFVD DDEDAFPNDP
     AASTDTDGDG MPDDWNPGYT ARDSESGLVL DLDDDNDGYS DKEEEEADTD SLNAADQPIS
     GMSILLIKQA IDSAAARSQQ
//
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