ID A0A0A7S8Z6_FRIPE Unreviewed; 605 AA.
AC A0A0A7S8Z6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=SurA N-terminal domain protein {ECO:0000313|EMBL:AJA45806.1};
GN ORFNames=DKK76_09855 {ECO:0000313|EMBL:PXY94461.1}, FPB0191_01995
GN {ECO:0000313|EMBL:AJA45806.1};
OS Frischella perrara.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Orbales; Orbaceae;
OC Frischella.
OX NCBI_TaxID=1267021 {ECO:0000313|EMBL:AJA45806.1, ECO:0000313|Proteomes:UP000030901};
RN [1] {ECO:0000313|EMBL:AJA45806.1, ECO:0000313|Proteomes:UP000030901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEB0191 {ECO:0000313|EMBL:AJA45806.1,
RC ECO:0000313|Proteomes:UP000030901};
RX PubMed=25527542;
RA Engel P., Vizcaino M.I., Crawford J.M.;
RT "Gut symbionts from distinct hosts exhibit genotoxic activity via divergent
RT colibactin biosynthetic pathways.";
RL Appl. Environ. Microbiol. 0:0-0(2014).
RN [2] {ECO:0000313|EMBL:PXY94461.1, ECO:0000313|Proteomes:UP000247838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ESL0167 {ECO:0000313|EMBL:PXY94461.1,
RC ECO:0000313|Proteomes:UP000247838};
RA Ellegaard K.M.;
RT "Reference genomes for bee gut microbiota database.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PpiD chaperone family.
CC {ECO:0000256|ARBA:ARBA00038408}.
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DR EMBL; CP009056; AJA45806.1; -; Genomic_DNA.
DR EMBL; QGLM01000020; PXY94461.1; -; Genomic_DNA.
DR RefSeq; WP_039105737.1; NZ_QGTI01000005.1.
DR AlphaFoldDB; A0A0A7S8Z6; -.
DR STRING; 1267021.FPB0191_01995; -.
DR GeneID; 78460366; -.
DR KEGG; fpp:FPB0191_01995; -.
DR HOGENOM; CLU_023843_1_1_6; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000030901; Chromosome.
DR Proteomes; UP000247838; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030901};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 225..345
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 605 AA; 68762 MW; F88E1878BF35572B CRC64;
MMEKLRTAAN SLIIKIIFGL IIVAFIFTGF GSFLDFGPNI ENDKQLYIAK INGEGISRAA
YEKELQMALK NSKNLSENDP LIKELSQSII SNLINDVLSY ELADSLDLNI SDEQVKNQIR
QQDIFFVNGA FNQERYLNIL ALANYTPDAY ANGLRSAMKK NQLLDALIST NFVIPKDSDI
SALFNQTRTV YLSNYGLSNV EGDFSVSDEE IKEYYNQNKQ SFNHPTRLKM EYLINPYPEI
KNKVMISNSM VEQYYADGKP GTMSLAKQSF SILSFNSLAK ANAEYKKLMA MKTKNRLNVK
MDDLGWFNKD DQIVSLLGNQ KLTAVGSISK PINQSGRYYI VRLDKIKEAQ KLPLNYVRGN
IIELLKTEEA NKIYNEQQIR LEKAAKLPTI DEISKASGLP VIQSKWTTEN ELYSIGRFPT
IHDIIFSDLM IKDGKPTNTI SDIIYAPEYQ SSFIIQVTDY QEPGIKDLEE VKDDIKDFLI
AKKKKENFAI DVENIIAKMN KEQSAGNVQF VQRATFSRNN NSNKLLNQDT IDKIFSVVPD
PKTGEVFGGT IENDINARLF VLTSIKDGQI TDISNQLQLD YMGFNYDYII DDLRSHAKIE
MMDDN
//
