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Database: UniProt
Entry: A0A2D8P4C7_9RHOB
LinkDB: A0A2D8P4C7_9RHOB
Original site: A0A2D8P4C7_9RHOB 
ID   A0A2D8P4C7_9RHOB        Unreviewed;       613 AA.
AC   A0A2D8P4C7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:MAM60286.1};
GN   ORFNames=CMH11_02225 {ECO:0000313|EMBL:MAM60286.1};
OS   Maritimibacter sp.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Maritimibacter.
OX   NCBI_TaxID=2003363 {ECO:0000313|EMBL:MAM60286.1, ECO:0000313|Proteomes:UP000224593};
RN   [1] {ECO:0000313|Proteomes:UP000224593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PpiD chaperone family.
CC       {ECO:0000256|ARBA:ARBA00038408}.
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:MAM60286.1}.
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DR   EMBL; NZNT01000010; MAM60286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D8P4C7; -.
DR   Proteomes; UP000224593; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   PANTHER; PTHR47529; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE D; 1.
DR   PANTHER; PTHR47529:SF1; PERIPLASMIC CHAPERONE PPID; 1.
DR   Pfam; PF13145; Rotamase_2; 1.
DR   Pfam; PF13624; SurA_N_3; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Isomerase {ECO:0000313|EMBL:MAM60286.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          243..361
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|Pfam:PF13145"
SQ   SEQUENCE   613 AA;  67167 MW;  6B853A7562982A5B CRC64;
     MFSNISRFFV WIIMALVVVG LVGFGSVNFG GSGQSIGKVG DTEIDASAYF RELNAELNAW
     QATTGENLTM AEAQAIGLDQ RVLSRVISIT ALEDEIDRMK LSVGDQNLAN RVTEIQAFQG
     VDGQFDRDTY DFVLQQSGLT AQEFEESLRA EVARTILADA VTSGVDVPDT YTATLYAWAR
     ETRDFTWAPV TRSALEEPLP EPTEADLQAF YDENPDPFTV PETRQITYGW LKPEDVMDEV
     PMDDGQLRDL YESRIDEFQV PERRLVERLV FGTEDDAQAA ADRIESGETT FDQEVEARGL
     TLSDVDLGDV RQRALGQAGE PVFALEEPGV VGPVMTDLGP ALLRMNAILS AQETSFEDAR
     DQLFEEYAAD AARRLVRTRA SEIDEMLAGG ATLEELDSEG LMPLDTIGWT EGMDDGIAAY
     APFREAAAEA SVNDFPQVTE LEDGSVFALR LDEITEPTLR PFDEVRDEVQ ALWEQNALAD
     ALVARAEALL PEFESGAEAP STVGLTEVLE EDVPRTAFIQ GAPENMVEQA FTMAEGSWQV
     VRGNGQVVVV GLTDIQSPDQ DSDEAQQIKS AFSQRMSQTL GLDLQDAFSS ALEDQAGVSL
     DQAMINAVHA NFP
//
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