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Database: UniProt
Entry: Q7UQJ9_RHOBA
LinkDB: Q7UQJ9_RHOBA
Original site: Q7UQJ9_RHOBA 
ID   Q7UQJ9_RHOBA            Unreviewed;      1541 AA.
AC   Q7UQJ9;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   SubName: Full=Probable cyclophilin type peptidylprolyl isomerase {ECO:0000313|EMBL:CAD74703.1};
DE            EC=5.2.1.8 {ECO:0000313|EMBL:CAD74703.1};
GN   OrderedLocusNames=RB6278 {ECO:0000313|EMBL:CAD74703.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD74703.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD74703.1, 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; BX294143; CAD74703.1; -; Genomic_DNA.
DR   RefSeq; NP_867158.1; NC_005027.1.
DR   STRING; 243090.RB6278; -.
DR   EnsemblBacteria; CAD74703; CAD74703; RB6278.
DR   KEGG; rba:RB6278; -.
DR   PATRIC; fig|243090.15.peg.3026; -.
DR   eggNOG; COG0526; Bacteria.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_246797_0_0_0; -.
DR   InParanoid; Q7UQJ9; -.
DR   OrthoDB; 270889at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00317; cyclophilin; 1.
DR   Gene3D; 2.60.40.2810; -; 3.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR044016; Big_13.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011506; Planctomycete_extracellular.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; NF012211; tand_rpt_95; 3.
DR   PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR   PANTHER; PTHR45625:SF4; PEPTIDYLPROLYL ISOMERASE DOMAIN AND WD REPEAT-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF19077; Big_13; 1.
DR   Pfam; PF17963; Big_9; 3.
DR   Pfam; PF05345; He_PIG; 1.
DR   Pfam; PF07595; Planc_extracel; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF49313; Cadherin-like; 1.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:CAD74703.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001025}.
FT   DOMAIN          260..403
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          75..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1541 AA;  159791 MW;  C0DFF2F3F5705661 CRC64;
     MNFDNSSRRP SASKHSFQSQ VRRRLMSWIQ GTSAAPSGEP VQRGRLQLES LEKRQMMAGD
     VELFATEGFF GSAGESSAAV ESSSTDRGTS DRAAEGEPGQ DLVQFAKDLD AAGVTFYGAH
     WCPACTQQKQ LFEDGGDDLP FVEVTLPDRT QDPQFSSLNI SEYPTWVFPD GTRLTGVQSL
     QTLSTRSGVA IPTSDNENPS FETIDAQTVE LGSPLHIPID GYDAEGGPLT VTVSVANPNL
     VEATVLSGNR SLRLDMDGFG DMVFELFEQR AARPTERVID LANSGFYDGL IFHRVVNGFV
     IQGGDPTGTG TGGSNLGDFD DEFHPDLQHN RTGVLSFAKS SDDTNDSQFF ITEVETDFLD
     FNHSVFGQLV EGEDVREAIS NMQVNNSTSN KPTTDIVINN ATVFNDTENS VIMLKGLGGT
     GSTTVTVTIT DSDGNSFDQI VPVTITDPPT DRRNAQPYLE DINVPASSPK TTPVELQLES
     FDLEGDAVQY FVSGGVTGGT ATVNASTGLL QVTPAANVSG TQTVSLTVGV AAASNAGSNS
     DLQSLVFTFT DSNTQAPAAP SSLDLRSSSD TGNSSGDNLT NAASLTFDVS GVTTGATVQI
     INTADNTVVG VGTATGGSIA ITTSNLAAIG DGTYSLAARQ IVGGVTSGTS TALSVTLDRT
     DPSFTLPANS STGNVGAAYQ ANLSSSEEGS GATYSLTVFP TGATIGSSTG IINWTPTAAQ
     LGSNDFTVEI RDLAGNTYTE SFSVTIAEEA LARLEVRLTD LDGNTIDSVD VGQEFFLQLI
     GVDARDLSER GGIYSAYADI EFDSSIADFV PGTSIEYDND FDFLPRGTLS SGLFNEIGAA
     SSRFSPTNLQ ESVMATVRMR AISDGSLTFT TNPADVSANE TLLFFNNDRL PAGSINYGST
     TLTVGDVTTN NPPVGVDDTF TVISGSGQNT LDVLANEAST ADPGETLTIT AVGTASNGGT
     LSIASNGLSI NYTPPANFIG TDTFQYTVSD GTSTDTVQVT VNIQSDDNAP TAVNDSFPAT
     GTILEDSNAV NYDVLANDTT DADNESFTIT GVGSASNGGQ VSIVNSGSGL SYKPAANFNG
     TETVTYTIRD TGGGLSTATV TFTVTAVNDA PLSENVTVDT VRGTSNEAVL TRGDLPANVD
     VGEVLQFVNL STPSAGGTVT VSSDGSSILY TPPSSTFTGT DTFTYQVQDA GGLSSSTATI
     TVNIADYLAR AFNFQFDSIG ALSSSFYEAA ILSGTNARGE SVSIPLSDSS VVVSGGTISV
     PDMLPGSYKL SIPAVPFFEG GEEAREIDIE SGADESDENL SLSFGRLLPQ YIRVNDWFGS
     APARRVVAAV LPGSNAFYMQ SSGAADSRLS DVELSLNAAG TSITVNATES TTANGATTTA
     QVSGTANLND GNALEVRGQV GEFRLLILNF DETGIELEAP TSSSTAAAST QSSTTQAAGE
     PLASAVTMAD ATVPVSELGT SRIQSSVEPA GEPIEVLSGD SEKVVAESDD ASQIDAAMPD
     VTDSLTRISD AEDVVASGVT GQPQLLGEAV DEVLTGVSGS N
//
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