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Database: UniProt
Entry: A0A1C4HZM5_9ACTN
LinkDB: A0A1C4HZM5_9ACTN
Original site: A0A1C4HZM5_9ACTN 
ID   A0A1C4HZM5_9ACTN        Unreviewed;       661 AA.
AC   A0A1C4HZM5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=TAP-like protein {ECO:0000313|EMBL:SCD30132.1};
GN   ORFNames=GA0115242_10197 {ECO:0000313|EMBL:SCD30132.1};
OS   Streptomyces sp. SolWspMP-5a-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1838281 {ECO:0000313|EMBL:SCD30132.1, ECO:0000313|Proteomes:UP000199131};
RN   [1] {ECO:0000313|EMBL:SCD30132.1, ECO:0000313|Proteomes:UP000199131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SolWspMP-5a-2 {ECO:0000313|EMBL:SCD30132.1,
RC   ECO:0000313|Proteomes:UP000199131};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; FMCI01000017; SCD30132.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4HZM5; -.
DR   OrthoDB; 9796770at2; -.
DR   Proteomes; UP000199131; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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        498..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        541..560
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        566..589
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        601..619
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        625..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          101..241
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          395..479
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
SQ   SEQUENCE   661 AA;  70038 MW;  E9FB4A0937925D38 CRC64;
     MRSSPHSRRS LVVAGISAAL LVLAAVVLWP DSPVRVPQGA AADSLTMKPC SYDTEDGSVP
     ADCGTLVVAE NRRDADSRLI ALPVVRIRAA SKPSGEPVFR FGGGPGQSNM DFPQAGRLRE
     KHDVVLVGYR GVDGSSRLDC DEVTDALQSA ADMTGEENLP HVRRAFERCA DRLQRGGADL
     TGYSAVQRVE DMESARKALG YRRIDLLSSS AGTRTAMIYA WRHPDALRRS AMISVNPPGH
     LFWDPRITDT QFGQYADLCR ADRACDAKTS DLAATIRTRI AELPSRWGPF SIKKTNISIL
     SQYSMHMNGE GSAPGNAPTV FDAYLDGGPG AMWAMSVLAD VTLPNSTVWG ELASFAMIDA
     PALRDYYAEG GDPGSILGNS ATDFLWGGPD GFPSVWPDSP DNADYRTVRP SSVETLLIGG
     ELDFSTPPVN ATKELLPSLS RGSEVIVPGI GHTADFWQQQ PEAATHLLTT FYDSGRVDSS
     RFERRPVDFT AVPMSMSLIA GVLLAAVTGG PLLGLLALAL LARRRRGRGA PGRRAGLWIR
     LLGTVPLGLA GWLLGLLFAW TLAPQWFLTS LPVVVPGTGL LVGLGVYLAR PAEDADGTHR
     ATAPALVLVG GWLGALLGAL AGSGFLIPAT AVLGAVAGAN ALLAARALRH RSPHAATAVT
     G
//
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