ID A5UX42_ROSS1 Unreviewed; 688 AA.
AC A5UX42;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=TAP domain protein {ECO:0000313|EMBL:ABQ91195.1};
GN OrderedLocusNames=RoseRS_2826 {ECO:0000313|EMBL:ABQ91195.1};
OS Roseiflexus sp. (strain RS-1).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ91195.1, ECO:0000313|Proteomes:UP000006554};
RN [1] {ECO:0000313|Proteomes:UP000006554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Roseiflexus sp. RS-1.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; CP000686; ABQ91195.1; -; Genomic_DNA.
DR AlphaFoldDB; A5UX42; -.
DR STRING; 357808.RoseRS_2826; -.
DR KEGG; rrs:RoseRS_2826; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_025429_0_0_0; -.
DR OrthoDB; 9796770at2; -.
DR Proteomes; UP000006554; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 28..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..571
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 591..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 629..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 666..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 111..270
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 423..513
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 688 AA; 75256 MW; A911A54409CDCD0C CRC64;
MYVSYILSHN FLIPEGVFVL IIIRQRSAML LVIILMLMVS FIASPVQSAT PTGTFQPDAC
MFKLPSGAVE GRDLECGWLQ VPERHERPDG PVIRLAVAII KSRAANRKPD PLVMLQGGPG
GSTIDTYTRT LFAPGNRLRD LLDRDIVLFD QRGALYSEPS LVCEEQWELV ERTIEQRLTY
EEADRLSLEA VTACRRRLER ERIDVSAFNS VENAADVAAL ARALGYEQIN LYGVSYGTLL
AQHVMRDHPG ILRSVVLDAV VPASVNYLTE TPRSQDRVYT ELFGACAADP GCRSAYPNLE
QSLVTVIERL NREPARVPIT DNETGKTYNA VLDGDSFASV LFQIMYSSGF IPAVPRIIDD
ATRNDFRVLG QVLPLIVFDR TFSLGMHYSV ICAEDADFTP EDAPLEGVRP FIALDARRSL
EGYLERCAVW QVEPLEPFVD EPVVSDVPTL VLSGRFDPIT PPAFGDVVAR TLSRAYVYTF
PDTGHAAVGS SACADTILAS FLDNPSQQPD ASCLAESTGL RFISPATVIF TPVAFALATF
DASGLMPFGA FLAALLTLLS AWLIWPLGWV FRLITGGEAP RPSAGATLAR WLIVLAGVTG
ATFVATVLVT FVQMALANDA TLFYGWPRSL TMLATIWTLP ALTVVVIVCA ALSWARGWWS
IAGRVYYTFL TLAAIGCTAT LAWMGVMV
//
