ID A0A0H3CAX1_CAUVN Unreviewed; 323 AA.
AC A0A0H3CAX1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Parvulin-like PPIase {ECO:0000256|ARBA:ARBA00018370};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase plp {ECO:0000256|ARBA:ARBA00030642};
DE AltName: Full=Rotamase plp {ECO:0000256|ARBA:ARBA00031484};
GN OrderedLocusNames=CCNA_03163 {ECO:0000313|EMBL:ACL96628.1};
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050 {ECO:0000313|EMBL:ACL96628.1, ECO:0000313|Proteomes:UP000001364};
RN [1] {ECO:0000313|EMBL:ACL96628.1, ECO:0000313|Proteomes:UP000001364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N {ECO:0000313|Proteomes:UP000001364};
RX PubMed=20472802; DOI=10.1128/JB.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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 Evidence={ECO:0000256|ARBA:ARBA00000971};
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000256|ARBA:ARBA00007656}.
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DR EMBL; CP001340; ACL96628.1; -; Genomic_DNA.
DR RefSeq; WP_012640650.1; NC_011916.1.
DR RefSeq; YP_002518536.1; NC_011916.1.
DR AlphaFoldDB; A0A0H3CAX1; -.
DR GeneID; 7331001; -.
DR KEGG; ccs:CCNA_03163; -.
DR PATRIC; fig|565050.3.peg.3089; -.
DR HOGENOM; CLU_034646_1_0_5; -.
DR OMA; YEQAKPT; -.
DR OrthoDB; 14196at2; -.
DR PhylomeDB; A0A0H3CAX1; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.1040; -; 1.
DR Gene3D; 3.10.50.40; -; 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; PTHR47245:SF2; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE HP_0175-RELATED; 1.
DR PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF13145; Rotamase_2; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:ACL96628.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001364};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..323
FT /note="Parvulin-like PPIase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007771599"
FT DOMAIN 150..240
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 286..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 34701 MW; 25188F50F425E1AC CRC64;
MALKTSFRLM GVLGAVACAL MIASCGQNKV AEKPPEPGDT AVARVNGQVI WASDVKREAV
AQGLISEGEP LDISSEVFRQ RLDEVIDQKL LAAEAVKRKL DKDPLAQRRL AAARERILGD
MLVEGVVEKA VTEDAIRKLY AEQQKLSKRS EEIRARQILV GSQAEAESIK KLLATGASFD
ALAMERSTDQ ATRFNGGDLG YFTLDVMPEA YGAALKDAQK GALIGPFAAE GGWVLVKVED
KRTEEPITLE AARPQIIRFL TYDQVRDILE KLRGSAKVEM MIGKSQELPA GSAQEPASAP
PELQGAAPAS APPAAQPAQS AKQ
//