ID M7NLL1_9BACT Unreviewed; 745 AA.
AC M7NLL1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Peptidyl-prolyl cis-trans isomerase surA {ECO:0000313|EMBL:EMR02670.1};
DE EC=5.2.1.8 {ECO:0000313|EMBL:EMR02670.1};
GN Name=surA_2 {ECO:0000313|EMBL:EMR02670.1};
GN ORFNames=ADICEAN_02209 {ECO:0000313|EMBL:EMR02670.1};
OS Cesiribacter andamanensis AMV16.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cesiribacteraceae;
OC Cesiribacter.
OX NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR02670.1, ECO:0000313|Proteomes:UP000011910};
RN [1] {ECO:0000313|EMBL:EMR02670.1, ECO:0000313|Proteomes:UP000011910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMV16 {ECO:0000313|EMBL:EMR02670.1,
RC ECO:0000313|Proteomes:UP000011910};
RX PubMed=23682146;
RA Shivaji S., Ara S., Begum Z., Srinivas T.N., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Cesiribacter andamanensis Strain AMV16T, Isolated
RT from a Soil Sample from a Mud Volcano in the Andaman Islands, India.";
RL Genome Announc. 1:E00240-13(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:EMR02670.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AODQ01000050; EMR02670.1; -; Genomic_DNA.
DR RefSeq; WP_009195602.1; NZ_AODQ01000050.1.
DR AlphaFoldDB; M7NLL1; -.
DR STRING; 1279009.ADICEAN_02209; -.
DR PATRIC; fig|1279009.4.peg.2240; -.
DR eggNOG; COG0760; Bacteria.
DR eggNOG; COG2885; Bacteria.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000011910; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 2.
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; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR47245:SF2; SLR0208 PROTEIN; 1.
DR Pfam; PF00639; Rotamase; 1.
DR Pfam; PF13616; Rotamase_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 2.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:EMR02670.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011910};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..745
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007921667"
FT DOMAIN 129..231
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT DOMAIN 236..339
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 745 AA; 84702 MW; 401E83DFFC78966D CRC64;
MKNTYWLALC CLLLAACKSQ QPSADNATTT PTLFSIAGEP VSEREFLYVY NKNNISRDTT
LQPTEDLRQY LDLYINFKLK VREAREKGLH QQASFQEELD SYKKQLARPY LTESSVTEQL
VNEAYQRMAT EINASHILIA VNPGAAPADT LAAYQKAQDM RQRAQQGADF GDLARRFSDD
PSAQSNRGNL GYFTALQMVY PFENTAYTTP VGAVSAPVRT RFGYHVLKVH DKRPSQGKIK
VAHLMVRTQP EMSAEEQAAA KARVDALYQQ LQQGESWEAL VRQFSEDRST APKGGELQPF
STGQMIPEFE KVAFTLKEKG SIAPPVQTPY GWHIIKLLER EGLPPLDDIR DELEARVSRD
SRSQLQEEAL IARLKKENGF SENKAALQAL LQQADSSLLQ GSWNYQPAPE VASQLLFSLA
DSSYTTGDFV AWLSEHPYNR QAAAPETLLN RLYQDWQKEE IIAYEEAHLE EKYEDYRMLV
QEYHDGILLF QLMEENVWAK ALEDTTGLQQ FFAQHQQNYQ WQERIEGLVL NAANETILQQ
AETLLASPPY RVASKTLAEP VAEKGALTPQ SRRELGMLMA SMLQRQDLQL QIEAPQETAA
LFRSHLQESG FEASRYKLTQ PAKKQPVSLS LLSSSPLALE QRFNAREPLN LQVISGPFER
GDHPVVDAIR WQPGRYRLAQ DGRQYLVVVQ EVVPPGPKTL DQARGQAITD YQHYLEQQWV
ARLRDTYEVR VNKKELDNLL ERQKN
//