ID A0A085A407_9ENTR Unreviewed; 273 AA.
AC A0A085A407;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN Name=fkpA {ECO:0000313|EMBL:KFC04952.1};
GN ORFNames=GTGU_03050 {ECO:0000313|EMBL:KFC04952.1};
OS Trabulsiella guamensis ATCC 49490.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=1005994 {ECO:0000313|EMBL:KFC04952.1, ECO:0000313|Proteomes:UP000028630};
RN [1] {ECO:0000313|EMBL:KFC04952.1, ECO:0000313|Proteomes:UP000028630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49490 {ECO:0000313|EMBL:KFC04952.1,
RC ECO:0000313|Proteomes:UP000028630};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) 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|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:KFC04952.1}.
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DR EMBL; JMTB01000093; KFC04952.1; -; Genomic_DNA.
DR RefSeq; WP_038158608.1; NZ_JMTB01000093.1.
DR AlphaFoldDB; A0A085A407; -.
DR eggNOG; COG0545; Bacteria.
DR OrthoDB; 9814548at2; -.
DR Proteomes; UP000028630; Unassembled WGS sequence.
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; 3.10.50.40; -; 1.
DR Gene3D; 1.10.287.460; Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR000774; PPIase_FKBP_N.
DR InterPro; IPR036944; PPIase_FKBP_N_sf.
DR PANTHER; PTHR10516; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR10516:SF464; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP12; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF01346; FKBP_N; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00277};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..273
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001786142"
FT DOMAIN 165..250
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 253..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 273 AA; 29306 MW; 4E3EFD9FE014C685 CRC64;
MKSFFKVTLL ATTMAVALNA PLAFAADAAK PAATAANSKA TFKNDDQKSA YALGASLGRY
MENSLKEQEK LGIKLDKDQL IAGVQDAFAN KSKLSDQEIE QTLQAFETRV KTSAQQKMEK
DAADNEAKGK TYRDTFAKEK GVKTSSTGLL YKVEKEGTGD APKDSDTVVV NYKGTLIDGK
EFDNSYTRGE PLSFRLDGVI PGWTEGLKNI KKGGKIKMVI PPDLAYGKTG VPGIPANSTL
VFDVELLDIK PAPKADAKPE AAADEKAAET SKK
//