ID SURA_HAEIN Reviewed; 313 AA.
AC P44721;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Putative peptidyl-prolyl cis-trans isomerase SurA;
DE Short=PPIase SurA;
DE EC=5.2.1.8;
DE AltName: Full=Chaperone SurA homolog;
DE AltName: Full=Rotamase SurA;
DE Flags: Precursor;
GN Name=surA; OrderedLocusNames=HI_0458;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Chaperone involved in the folding of extracytoplasmic
CC proteins. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
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DR EMBL; L42023; AAC22116.1; -; Genomic_DNA.
DR PIR; F64069; F64069.
DR RefSeq; NP_438619.1; NC_000907.1.
DR AlphaFoldDB; P44721; -.
DR SMR; P44721; -.
DR STRING; 71421.HI_0458; -.
DR EnsemblBacteria; AAC22116; AAC22116; HI_0458.
DR KEGG; hin:HI_0458; -.
DR PATRIC; fig|71421.8.peg.478; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_11_0_6; -.
DR OrthoDB; 14196at2; -.
DR PhylomeDB; P44721; -.
DR BioCyc; HINF71421:G1GJ1-474-MONOMER; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0042597; C:periplasmic space; 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; IPR015391; SurA_N.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47637; CHAPERONE SURA; 1.
DR PANTHER; PTHR47637:SF1; CHAPERONE SURA; 1.
DR Pfam; PF00639; Rotamase; 1.
DR Pfam; PF09312; SurA_N; 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 Chaperone; Isomerase; Periplasm; Reference proteome; Rotamase; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..313
FT /note="Putative peptidyl-prolyl cis-trans isomerase SurA"
FT /id="PRO_0000025543"
FT DOMAIN 167..267
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ SEQUENCE 313 AA; 34670 MW; EAE2A7C352302450 CRC64;
MKMKKFVLRS FLLATLGCVA FTSMAQAEER VVATVDGIPV LESQVRANMG KKGDRQSAID
KIIDDILVQK AVQESGVKID PREIDHIVED TAARNGLTYG QFLDALDYQG ISLNTFRQQI
ANQMVMGAVR NKAIQESIDV TREEVVALGQ KMLDEAKSQG TAQKVTGKEY EVRHILLKLN
PLLNDAQAKK QLAKIRSDII AGKTTFADAA LKYSKDYLSG ANGGSLGYAF PETYAPQFAQ
TVVKSKQGVI SAPFKTEFGW HILEVTGVRD GDLTAEAYTQ KAYERLVNTQ LQDATNDWVK
ALRKRANIQY FNK
//
