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Database: UniProt
Entry: K6XXV9_9ALTE
LinkDB: K6XXV9_9ALTE
Original site: K6XXV9_9ALTE 
ID   K6XXV9_9ALTE            Unreviewed;       143 AA.
AC   K6XXV9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   Name=mip {ECO:0000313|EMBL:GAC16491.1};
GN   ORFNames=GLIP_3880 {ECO:0000313|EMBL:GAC16491.1};
OS   Aliiglaciecola lipolytica E3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Aliiglaciecola.
OX   NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC16491.1, ECO:0000313|Proteomes:UP000006334};
RN   [1] {ECO:0000313|EMBL:GAC16491.1, ECO:0000313|Proteomes:UP000006334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3 {ECO:0000313|EMBL:GAC16491.1,
RC   ECO:0000313|Proteomes:UP000006334};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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, ECO:0000256|PROSITE-
CC         ProRule:PRU00277, ECO:0000256|RuleBase:RU003915};
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC       {ECO:0000256|ARBA:ARBA00006577, ECO:0000256|RuleBase:RU003915}.
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:GAC16491.1}.
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DR   EMBL; BAEN01000076; GAC16491.1; -; Genomic_DNA.
DR   RefSeq; WP_008846293.1; NZ_BAEN01000076.1.
DR   AlphaFoldDB; K6XXV9; -.
DR   STRING; 1127673.GLIP_3880; -.
DR   eggNOG; COG0545; Bacteria.
DR   OrthoDB; 9814548at2; -.
DR   Proteomes; UP000006334; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProt.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR43811:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1.
DR   PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|RuleBase:RU003915};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006334};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}.
FT   DOMAIN          57..143
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   143 AA;  15735 MW;  DE5412A61C8A4403 CRC64;
     MGKQKQKKTA KGSTGHNKNL TADFINKYQG RADVSATGSG LLYTIIDMSD GQKPQIPNIV
     RVNQRILLAD GSVIDDTYKT GIPEEFSLEE AIEGLREGIQ LMPVGSRFEF VIPPELAWGK
     KGNRSKIGPN TVMIVDVRLI SFE
//
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