ID A0A1A9T4L6_9PROT Unreviewed; 633 AA.
AC A0A1A9T4L6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=A7981_05815 {ECO:0000313|EMBL:OAM52947.1};
OS Methylovorus sp. MM2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylovorus.
OX NCBI_TaxID=1848038 {ECO:0000313|EMBL:OAM52947.1, ECO:0000313|Proteomes:UP000077545};
RN [1] {ECO:0000313|Proteomes:UP000077545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM1 {ECO:0000313|Proteomes:UP000077545};
RA Macey M.C., Murrell J.C.;
RT "Draft genome of Methylovorus sp. MM1 isolated from grassland soil.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004382}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004382}; Periplasmic side
CC {ECO:0000256|ARBA:ARBA00004382}.
CC -!- SIMILARITY: Belongs to the PpiD chaperone family.
CC {ECO:0000256|ARBA:ARBA00038408}.
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:OAM52947.1}.
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DR EMBL; LXUF01000001; OAM52947.1; -; Genomic_DNA.
DR RefSeq; WP_067265271.1; NZ_LXUF01000001.1.
DR AlphaFoldDB; A0A1A9T4L6; -.
DR STRING; 1848038.A7981_05815; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000077545; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
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; PF13616; Rotamase_3; 1.
DR Pfam; PF13624; SurA_N_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:OAM52947.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077545};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 264..367
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 633 AA; 69614 MW; 73D0A0291F859609 CRC64;
MLDAIREHSK GWLAKVILAA ITIPFALVGI DTYLRDAGSN VPIAKVGSES ISVQEYGNSL
QKLRNQLQEE GKTDPSVLDN PDVKRSILDR LIATKLINAE ANHLRFIISD DQVHQYLLNM
PQFQQDGAFS EDLYYRLLSS NRMSASQFEN SLRADMLLQQ TRQGIVATAY NTKAAAEHAL
SIEHQQREVS VAEIKTADFL TQVKVDPAEV KAFYDKHQDN FRVPDQVKLE FVLMSASSLI
QGIQVTDQEV KQEFEKNASK FQGDEQRQAS HILIGFGVSA TPETKQAAKK KAQEILAEVK
QSPTKFAELA KKYSQDPGSK DKGGDLGAFG RGMMVKPFED AVYSMQPGQV SDLVESEFGY
HIIKLTGITG QAQSFDAVKA QLKGDLLYQK ALAKFSEQAE NFSNMVYEQS TSLQPVADAF
GIQVQTSAWL TRADGAKFFK SDKLMNSVFS DEVLKDRRNT EAVEVSSNNL VAARVVDYKP
ASPRTFDEVK AGIEDYLKLE KASKLAAEKG EAALAGLKQG KDADHLEWIP PVTVDRKNAQ
GLTELTMSNV FKIDTSKLPA YTGALNSNKG YQLIKVTKVS SELAEDDSAK KAAAAELKSA
LAAEYLAAYV ESLKAKAKVN INEQLLSAGS LTQ
//
