(data stored in ACNUC7421 zone)
SWISSPROT: A4AVJ7_MARSH
ID A4AVJ7_MARSH Unreviewed; 310 AA.
AC A4AVJ7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 08-MAY-2019, entry version 81.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN OrderedLocusNames=FB2170_01095 {ECO:0000313|EMBL:EAR00219.1};
OS Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00219.1, ECO:0000313|Proteomes:UP000001602};
RN [1] {ECO:0000313|EMBL:EAR00219.1, ECO:0000313|Proteomes:UP000001602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX PubMed=21037013; DOI=10.1128/JB.01207-10;
RA Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA Cho J.C.;
RT "Complete genome sequence of strain HTCC2170, a novel member of the
RT genus Maribacter in the family Flavobacteriaceae.";
RL J. Bacteriol. 193:303-304(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000256|PROSITE-
CC ProRule:PRU00277, ECO:0000256|RuleBase:RU003915};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|RuleBase:RU003915}.
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DR EMBL; CP002157; EAR00219.1; -; Genomic_DNA.
DR RefSeq; WP_013304914.1; NC_014472.1.
DR STRING; 313603.FB2170_01095; -.
DR EnsemblBacteria; EAR00219; EAR00219; FB2170_01095.
DR KEGG; fbc:FB2170_01095; -.
DR eggNOG; ENOG4108V1T; Bacteria.
DR eggNOG; COG0545; LUCA.
DR eggNOG; COG0652; LUCA.
DR HOGENOM; HOG000025706; -.
DR OMA; GIYAKFN; -.
DR OrthoDB; 1861282at2; -.
DR BioCyc; MSP313603:G1GNS-483-MONOMER; -.
DR Proteomes; UP000001602; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
DR PRODOM; A4AVJ7.
DR SWISS-2DPAGE; A4AVJ7.
KW Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000256|RuleBase:RU003915, ECO:0000313|EMBL:EAR00219.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000256|RuleBase:RU003915}.
FT DOMAIN 14 148 PPIase cyclophilin-type.
FT {ECO:0000259|PROSITE:PS50072}.
FT DOMAIN 222 310 PPIase FKBP-type. {ECO:0000259|PROSITE:
FT PS50059}.
SQ SEQUENCE 310 AA; 33517 MW; AD4CAEB195F33031 CRC64;
MQDGIYAKFN TSKGEILVKL THDKTPGTVG NFVALAEGKL ENKAKSTGEP YYNGLKFHRV
IPDFMIQGGC PLGTGTGDPG YKFDDEFHPE LTHDTPGVLS MANAGPGTNG SQFFITHVPT
PWLDNKHTVF GHVEAGQEVV DVIAQADSIE SLEIVRVGDE AEKWDALGSF KSFESSREKR
MAEEKERQVA ELDKVAAGFD ETESGLRYKI IQKGTGDKAE SGRTVSVHYE GSLLSGQVFD
SSYKRNQPID FQLGVGQVIA GWDEGISLLV VGDKARFVIP SNLGYGSAGA GGVIPPDATL
IFDVELMEVK
//
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