ID A0A0V8HZI4_9MICC Unreviewed; 312 AA.
AC A0A0V8HZI4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=AS038_02015 {ECO:0000313|EMBL:KSU67890.1};
OS Arthrobacter sp. NIO-1057.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=993071 {ECO:0000313|EMBL:KSU67890.1, ECO:0000313|Proteomes:UP000054434};
RN [1] {ECO:0000313|EMBL:KSU67890.1, ECO:0000313|Proteomes:UP000054434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIO-1057 {ECO:0000313|EMBL:KSU67890.1,
RC ECO:0000313|Proteomes:UP000054434};
RA Dastager S.G., Mawlankar R.B., Thorat M.N., Jiao J.-Y., Sonalkar V.,
RA Li W.-J.;
RT "Arthrobacter sp NIO-1057.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00000971, ECO:0000256|PROSITE-
CC ProRule:PRU00277, ECO:0000256|RuleBase:RU003915};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00006577, ECO:0000256|RuleBase:RU003915}.
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:KSU67890.1}.
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DR EMBL; LNQJ01000001; KSU67890.1; -; Genomic_DNA.
DR RefSeq; WP_058254295.1; NZ_KQ758454.1.
DR AlphaFoldDB; A0A0V8HZI4; -.
DR STRING; 993071.AS038_02015; -.
DR Proteomes; UP000054434; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR43811:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1.
DR PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000256|RuleBase:RU003915};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..312
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039364587"
FT DOMAIN 222..307
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 20..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 32436 MW; 484E40C212362D14 CRC64;
MRKVLALCAT ASVLALAACG SGSSSDLSSI SVKPAADDNT APEVSFDTPF LTEKDEAVTL
EQGDGAEINA GDTVSIKSGL YKAIDGLSAG ENFTGTATEM TVDDSMKQQM PELYDRLVDS
KVGDWIAYST VEGTQQSDGT VADPEEGARA ERIIVLHVES STAASGTMSK DEVAKQKKDG
KLPTVKVTDG KPTITIPKDT DAPKDLVVDV LEEGKGEAAT ATSKVKAKYT GVTWADGTEF
DGNFDADEGT EFSLDGVIKG WTEGMTGLKA GSKVLLTIPA DKAYGNSSTS GSPTGTLVFY
VELESVTAGD SE
//
