ID   Q7UF12_RHOBA            Unreviewed;      1352 AA.
AC   Q7UF12;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN   OrderedLocusNames=RB10413 {ECO:0000313|EMBL:CAD78871.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD78871.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD78871.1, ECO:0000313|Proteomes:UP000001025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC   {ECO:0000313|Proteomes:UP000001025};
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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DR   EMBL; BX294151; CAD78871.1; -; Genomic_DNA.
DR   RefSeq; NP_869414.1; NC_005027.1.
DR   EnsemblBacteria; CAD78871; CAD78871; RB10413.
DR   KEGG; rba:RB10413; -.
DR   PATRIC; fig|243090.15.peg.5038; -.
DR   eggNOG; COG1404; Bacteria.
DR   HOGENOM; CLU_257590_0_0_0; -.
DR   InParanoid; Q7UF12; -.
DR   OrthoDB; 9813435at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05562; Peptidases_S53_like; 1.
DR   Gene3D; 2.60.40.2080; -; 2.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR034075; Glr3161-like_dom.
DR   InterPro; IPR037221; H-type_lectin_dom_sf.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   PANTHER; PTHR35533; CONSERVED REPEAT DOMAIN PROTEIN; 1.
DR   PANTHER; PTHR35533:SF13; CONSERVED REPEAT DOMAIN PROTEIN; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001025}.
FT   DOMAIN          559..646
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          243..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..683
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1352 AA;  142714 MW;  1E6C675F535B950E CRC64;
     MAIRTLVTKL LQTGNLDSFL TPNSSPPVIQ SGVSSRRASV RRKRSMQCEP LERRELLAAE
     VLPEIRSFAD FPAFLSGSSN AALIQSESSA FTQTISSNDF SEFWEASDPT ELISVEIRVD
     DAFSTQDAQA ALAELDFEKT ASFGWNLEGY LARGKMVEAA ELPMVQVVRE NSAAIFNAGT
     VFSQADPAMR SNLARSQFNV NGAGIKIGVI SDSYSRTNGG GGASGSVASG NLPGSGNPNG
     FTIPVTVLQD APTTGPTAGN GKDEGRAMLE LIHDIAPGAQ LFFHTAITGP VQFAEAVQAL
     SAAGVDIIVD DVTYAGMQIF QDGVTAQAVA QATSAGISFF SSAGNQGSEA YSALYHTDGR
     TSTIPNFPPS AGKVYEPHDF DPGPGVDNFQ RVVLGSGRST TITFQWDQPS ASLGGPGAST
     DMDIIVFNEF GTPVSGGVQN NVGQDPIEIF ALSNPTNSPL ILEVGIFRNV SAGGPRPSIV
     HYHPLTSPTD FDIFQFETLG GTLFGHHQAP GVAAIAAVDY RQTPAFGVSP PGVQESTSEG
     GLPILFDTAG NRLATPEIRT QPVVTAPDTI NNSFFGSPLD VEGDGIFNFA GTSAAAPNAA
     AVAALMLQAA GGRGSLTPAQ IRAAMANTAI DIPLTGNGFD HFTGFGLIDA NAAVAAVRNT
     NPPPPPPPPP PPPPPPPNPP SPSLIDREIG ESGNTRVDQD WKTIQLQNAY VDPVVIASPA
     SFGGPDPVTV RIRNVTSNSF QVRLQEWDYD DGNHSLETVS YLVVEKGSYA LPDGRVLHAG
     TTSVNQNLKR VDFPDIFETS PVVLSQSQTV NGPSAIVTRQ QEISRTGFRV RVQEEQGADG
     NHSTERVGYI AIEAGAGNAA GTSYRVGRTG ERISEAFASI NLGTGFDAPP AFLAAMQTTT
     GADPAGLRFR NLGKNSVQVF VEEEQSADAE TSHSDENVGF AAFEIGALVG QPVEVVGESG
     TFRVDQDWKT IQLQNAYVDP VVIASPASFG GPDPVTVRIR NVTSNSFQVR LQEWDYDDGN
     HSLETVSYLV VEKGSYALPD GRVLHAGTTS VNQNLKRVDF PDIFETSPVV LSQSQTVNGP
     SAIVTRQQEI SRTGFRVRVQ EEQGADGNHS TERVGYVAIE AGAGNAAGTS YRVGRTGERI
     SEAFASINLG AGFDAPPAFL AAMQTTTGAD PAGLRFRNLD KNSVQVFVEE EQSADAETGH
     SDENVGFAAF EIGAILARAA TSNASLNQAV TMSSSNAASY DNNNDVAMDS NRDGSISALD
     ALIIINFLSH SSMSEPIDVG VSNMALTFDA NEDGFVTARD ALVVINYLTK QSVIGSKTDE
     SKTVPRWDAD EVFASDEDFL LEHNLGISTD LF
//