ID F7RXJ7_9GAMM Unreviewed; 763 AA.
AC F7RXJ7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Dipeptidyl aminopeptidase/acylaminoacyl peptidase {ECO:0000313|EMBL:EGN75363.1};
GN ORFNames=A28LD_0976 {ECO:0000313|EMBL:EGN75363.1};
OS Idiomarina sp. A28L.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=1036674 {ECO:0000313|EMBL:EGN75363.1, ECO:0000313|Proteomes:UP000053031};
RN [1] {ECO:0000313|EMBL:EGN75363.1, ECO:0000313|Proteomes:UP000053031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A28L {ECO:0000313|EMBL:EGN75363.1,
RC ECO:0000313|Proteomes:UP000053031};
RX PubMed=21742887; DOI=10.1128/JB.05648-11;
RA Gupta H.K., Singh A., Sharma R.;
RT "Genome Sequence of Idiomarina sp. Strain A28L, Isolated from Pangong Lake,
RT India.";
RL J. Bacteriol. 193:5875-5876(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
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:EGN75363.1}.
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DR EMBL; AFPO01000012; EGN75363.1; -; Genomic_DNA.
DR RefSeq; WP_007419953.1; NZ_AFPO01000012.1.
DR AlphaFoldDB; F7RXJ7; -.
DR STRING; 1036674.A28LD_0976; -.
DR MEROPS; S09.013; -.
DR PATRIC; fig|1036674.4.peg.964; -.
DR eggNOG; COG1506; Bacteria.
DR OrthoDB; 9812921at2; -.
DR Proteomes; UP000053031; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF200; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 2; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:EGN75363.1};
KW Hydrolase {ECO:0000313|EMBL:EGN75363.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000313|EMBL:EGN75363.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053031};
KW Signal {ECO:0000256|SAM:SignalP};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..763
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003367751"
FT DOMAIN 120..471
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 564..758
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 763 AA; 86556 MW; 1138823DCE81372A CRC64;
MMKTTKIIAL AAGASLLLSA CATSPEMPSP RGQASPMPAD TTFSLADIYA SDMFSAKSFP
TTRWLADGSG YTTLESAEDG GRDIVRYHPE TEERTVLVYA AQLQPEGAEE PLRIANYEWS
EDGKQLLIFT NTKRSWRTHT LGDYWVLNLE NGRLVQLGAD FPASTLQFAK FDPAGSRVAY
VMQNNIYVQD LASLDITQIT SDGSSTIING TFDWVNEEEF SLRDGFRWSP DGEHIAYWQL
DTSGVPMFTM IDNVSELYPT LTEFPYPKVG ETNSELRVGT ISASGGDTTW VQLPGDPRQN
YIVRMEWAGN SDELMVQHMN RAQNNMQFWL AERATGEAVS LITEQSNAWV EQVDDVRFFR
DGQSFLWQSE RSGYRHLYRF DRDGNGLTPL TEGDYDIVQM LEIVADEQGN GYAWFIASPE
NPLQRYLFRV DLSGETPAER ITPQDWPGYH GYTVSRDGRF ALHTVTRMGV PTETRMVRLP
DHSVINELEM NTELKEVLAE KLTADVEFFQ VEARDGLMLD GYLKRPADFD PSKKYPLIMH
IYGEPWGQTV ADRWLGQTHL WHDYMTQLGY VVVSIDNRGT RSPRGQEWRH SIYMQLGIIT
VRDQADALDQ MLARWDWIDG NRVGMWGHSG GGSQTLNALF RYPEKFHAGV ALAPVPDLRL
YDTIYQERYS GLLPDAAESY EETSAVTHAA NLQGSLLLVH GTADDNVHYQ GSERLQDELI
KHNKQFRFMG YPNRTHGIRE GEGTSLHLRT MVTEFFWESI PVK
//
