ID D6E7Z9_9ACTN Unreviewed; 1555 AA.
AC D6E7Z9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Cysteine protease {ECO:0000313|EMBL:CBL03846.1};
GN ORFNames=GPA_11620 {ECO:0000313|EMBL:CBL03846.1};
OS Gordonibacter pamelaeae 7-10-1-b.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Gordonibacter.
OX NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL03846.1, ECO:0000313|Proteomes:UP000008805};
RN [1] {ECO:0000313|EMBL:CBL03846.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Timmis K., Oxley A., Wurdemann D.;
RT "The genome sequence of Gordonibacter pamelaeae 7-10-1-bT.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL03846.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; FP929047; CBL03846.1; -; Genomic_DNA.
DR RefSeq; WP_015539196.1; NC_021021.1.
DR KEGG; gpa:GPA_11620; -.
DR PATRIC; fig|657308.3.peg.742; -.
DR HOGENOM; CLU_246173_0_0_11; -.
DR BioCyc; GPAM657308:GPA_RS05355-MONOMER; -.
DR Proteomes; UP000008805; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd02619; Peptidase_C1; 2.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR040528; Lectin-like.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR PANTHER; PTHR12411:SF741; CATHEPSIN K; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF18560; Lectin_like; 2.
DR Pfam; PF00112; Peptidase_C1; 2.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000313|EMBL:CBL03846.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:CBL03846.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008805};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1555
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003083687"
FT TRANSMEM 1506..1527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..340
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT DOMAIN 835..903
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|SMART:SM00060"
FT REGION 738..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1535..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1555 AA; 164604 MW; 08919EC5DA3DF517 CRC64;
MIVRRMLALL LSAALVGGLA PGAALPAHAT EPNDGAAAQS AAIELTASDV NPDYLAYLNG
ETDIKASTLD LSYLGDTLAS GVATTFANDL LPESFDLRER GVVGPVLDQS QTQNCWAFAN
LGAAESSVLP YYPTAQLSRA HLAWFTYNGN EEQEVEGAKS YPQQAYDTGA WDQQAIGTLA
AWKGPVLSSR VPFQAAYVDE SLRYAADFHL QDAYYLPTSL NGITGAAMKP SIDTVKRIIH
DEGPVTVSIA THGNHWHGTE FVEGVSRQTM YASQKIDIDH AVLIVGWDDT FSRANFGGPE
TELPENDGAW LVKNSWGANW GESGYFWLSY EDHSAIYGAT LKLESKDNYT GNYQFDTMGW
RTSLAVSSGA GAEDPDAPSS GEGAAAYLAN VFTAAGNETL EAASFYTTDE GTSYAIDVYL
NPAEGDPTSG TKMGGTQTGS EAYPGYHTVE LDADLRSSLQ KGDTFSLVVK LENPFYKNVV
PAEAVIGRGA AFQPVYVGKD AAGNEEVSYV SADGISWTTL GKSLMDSKGT SVYATNVCLK
ALTREAGGSG AVWPPEEPDT SQVNGITVRS TLHETQGEFP LDLPAYEYLD LRSTLEEGGL
RTSFDVFLPA APSSAEGFSY SVSVLPTSNQ KVAMSFDGGA PEPLENGRFG REVALDDVVS
RTHTITLTSN DPAGLKGSTT YELRLCLSGL TFDNTTETVG FDDARLSVQA PDGTWLSNGD
RVSAWSVVDG LQPHHLSVFD RNDPDGEPRY RVPVPTREPD PTPGAITIDF TRETPNINTS
SKSLKASYQA DMSDSFPLFE DTPLEPGRRL YFRSGGLSGR FDSTGISYLD VPARPAAPTE
VAVREATSTS ITLAFQPDGQ QLEYRLADGS SQHDGWQSSC LFRDLQPETD YLFQVRKAAV
MPGGAGQGGL GSDGGDAKNA ERTDDGRVDA AALQEGAFAS EAVEMSARTA EALPSSFDLR
MTGALAPLRD QGVYSTCWAF AALASLESNR IAQGNADSSI DLSEASLAML TYQHRALGEG
DPSALDRYAV STKDEGLGAR GLLTGGTWSH AVSTLARWQG AADEGACPYL PPSEPGDYEE
AAAAMDAAAG TTVGSDAVRL DQAIELPSPF ATGSGGTGPA GGEINEPASS YAGDASSGAG
VAIDLLACEK IKEALRQYGA LDFGMHEPFE GDGYWADADV EQGIWKHHWF YDADTANYTV
NHSLSLVGWD DAYPKENFTI VVDGVEHTPA NNGAWILRNN RGEGFGDGGY LYVPYEERAI
RAPVALAAES GRDNTFDYAK NYQYDSLHAV GLQASWGDAA KAANVFTSSG DERLVGVGVW
VTSPAVRVTI DVYTGLADPT DPESGTQVTA AHTELDALNA GYLTPALANA VDLKKGQAFA
VVVTETQLYD QQGWALMSST IPLEGARQVG ENPDGTPRYD SVPHVDAGQS FVFEHGVWSD
VAAVADDLAA RTGSPVGNVA VKAFTNPAGT PVEPDGPPSP AGPDTEDSGN GGSDEARALV
RTGDTAVPAA IGALALAVLA ACAALAATAK REVTSSGSLL SRRASRRTCR LRPRE
//
