ID A0A095SMQ2_9GAMM Unreviewed; 253 AA.
AC A0A095SMQ2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=Y5S_00428 {ECO:0000313|EMBL:KGD65956.1};
OS Alcanivorax nanhaiticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177154 {ECO:0000313|EMBL:KGD65956.1, ECO:0000313|Proteomes:UP000029444};
RN [1] {ECO:0000313|EMBL:KGD65956.1, ECO:0000313|Proteomes:UP000029444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=19-m-6 {ECO:0000313|EMBL:KGD65956.1,
RC ECO:0000313|Proteomes:UP000029444};
RA Lai Q., Shao Z.;
RT "Genome Sequence of alkane-degrading Bacterium Alcanivorax sp. 19-m-6.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC proteins. Acts by transferring its disulfide bond to other proteins and
CC is reduced in the process. {ECO:0000256|RuleBase:RU364038}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC ECO:0000256|RuleBase:RU364038}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {ECO:0000256|ARBA:ARBA00009813, ECO:0000256|RuleBase:RU364038}.
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:KGD65956.1}.
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DR EMBL; ARXV01000002; KGD65956.1; -; Genomic_DNA.
DR RefSeq; WP_035230093.1; NZ_ARXV01000002.1.
DR AlphaFoldDB; A0A095SMQ2; -.
DR STRING; 1177154.Y5S_00428; -.
DR PATRIC; fig|1177154.3.peg.432; -.
DR eggNOG; COG1651; Bacteria.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000029444; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR Gene3D; 3.10.450.70; Disulphide bond isomerase, DsbC/G, N-terminal; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR InterPro; IPR018950; DiS-bond_isomerase_DsbC/G_N.
DR InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR35272:SF3; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC; 1.
DR PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR Pfam; PF10411; DsbC_N; 1.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF54423; DsbC/DsbG N-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:KGD65956.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 19..253
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010004266"
FT DOMAIN 42..94
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 126..252
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 253 AA; 27705 MW; EA09AABDAD485033 CRC64;
MKKWFVFALL GLVAACGAES GGKAAEASSA RGEAVNGDKA RAVFEKAFDG VTVSDVRNSP
IDGMLELEVD GSETVFITED GSYLLVGKLL QIKDGDVVNP AEERLEKVRK EGISKLDEAQ
MITYPAENEK YEIYVFTDIT CGYCRKLHRH IEEYNDEGVT VHYLAFPRGG SMAKAAEAMR
HIWCAEDRQA ALTKAKLNDD ISKAELGVCA KPVDEQYQLG VKFGVRGTPA IYTTEGKQLG
GYVAPDDLLK RLN
//