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Database: UniProt
Entry: N1UVP6_9MICC
LinkDB: N1UVP6_9MICC
Original site: N1UVP6_9MICC 
ID   N1UVP6_9MICC            Unreviewed;       261 AA.
AC   N1UVP6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Peptidylprolyl isomerase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=D477_016475 {ECO:0000313|EMBL:EMY33135.1};
OS   Arthrobacter crystallopoietes BAB-32.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1246476 {ECO:0000313|EMBL:EMY33135.1, ECO:0000313|Proteomes:UP000010729};
RN   [1] {ECO:0000313|EMBL:EMY33135.1, ECO:0000313|Proteomes:UP000010729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAB-32 {ECO:0000313|EMBL:EMY33135.1,
RC   ECO:0000313|Proteomes:UP000010729};
RX   PubMed=23833141;
RA   Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Desai S.M., Saxena A.K.,
RA   Bagatharia S.B.;
RT   "Draft Genome Sequence of Arthrobacter crystallopoietes Strain BAB-32,
RT   Revealing Genes for Bioremediation.";
RL   Genome Announc. 1:e00452-13(2013).
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:EMY33135.1}.
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DR   EMBL; ANPE02000197; EMY33135.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1UVP6; -.
DR   OrthoDB; 4775280at2; -.
DR   Proteomes; UP000010729; Unassembled WGS sequence.
DR   Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR   PANTHER; PTHR47245:SF2; SLR0208 PROTEIN; 1.
DR   Pfam; PF13624; SurA_N_3; 1.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000010729};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..261
FT                   /note="Peptidylprolyl isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038893213"
FT   REGION          25..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   261 AA;  28174 MW;  2AB936EBF5D1B680 CRC64;
     MSSNKWLVAI VVAGTLALTA CGGATEAGSA GQTQQASPGA SGQAQDPSAG QQEMPKPDLN
     GIPDVVAEVN GTKITKEDFT TAYEAQFQQM AMQSQMMGQE VDQEKLKKQT AEGIVGTELL
     IQEAGNRGLE ASQKETDKAL DEIVKTNQLK SKDEFMAAME KQGMDEAKVT EELKNQVMVE
     KLIAEEAGDT KPTDKELKAA YEEAKKQQEQ MAQQGGQGAE MPSFEESKPQ LEQQLKSQKE
     GEIVQALAKD LRAKADVKIH V
//
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