ID A1SBM1_SHEAM Unreviewed; 507 AA.
AC A1SBM1;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Hydrolase, alpha/beta hydrolase fold family {ECO:0000313|EMBL:ABM01778.1};
GN OrderedLocusNames=Sama_3575 {ECO:0000313|EMBL:ABM01778.1};
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297 {ECO:0000313|EMBL:ABM01778.1, ECO:0000313|Proteomes:UP000009175};
RN [1] {ECO:0000313|EMBL:ABM01778.1, ECO:0000313|Proteomes:UP000009175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175};
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) 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; CP000507; ABM01778.1; -; Genomic_DNA.
DR RefSeq; WP_011761681.1; NC_008700.1.
DR AlphaFoldDB; A1SBM1; -.
DR STRING; 326297.Sama_3575; -.
DR ESTHER; sheam-a1sbm1; Proline_iminopeptidase.
DR KEGG; saz:Sama_3575; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_025429_1_0_6; -.
DR OrthoDB; 4510475at2; -.
DR Proteomes; UP000009175; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; 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 InterPro; IPR002410; Peptidase_S33.
DR PANTHER; PTHR43798:SF27; HYDROLASE ALPHA_BETA HYDROLASE FOLD FAMILY; 1.
DR PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ABM01778.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009175};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..507
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002637378"
FT DOMAIN 95..246
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 379..478
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 507 AA; 54699 MW; F8633FDF36B3E5AA CRC64;
MKLRNLRQLA HKAPRLAGAA LLAMMALKSH AMATDILERP ASDGPQSCYL KDIADRALCG
LVTVPENPAK PDGKQINIHY AVLPAIKPSF PGEAFLAIAG GPGQSAIDNA AGFNNMFRKV
RQTRDILLID QRGTGRSNLL ACSDKGLDPL AIDDENADMI AETRKCLAAQ DADISQYGSV
TALGDFEAVR KALGYQKLHI YGVSYGSRMG QLYLRHYPEA LATVTLDGVV PMQQSVLAIG
EAIDRAVELM LKDCRENTAC QARFPALADE LAAVHSRLAQ SPVDIGVNHP LTGEPQQFLL
TRSKFAGVVR LALYSPTTRA LLPLAIHEAA KGNYQSILGL YGMTLGSLDL ASGMHNSVVC
GEDMHRIDAD LQQRLQQSYY GKLMLDGLQK ACSVWQVPAM ESNFAEAVDT KLPVLLLSGE
LDPATPPSWA EMAMAEMHNA RHLVAPYSGH GIARESCASG IIAEFVSEGA VDTLETDCLQ
KDIRRGFYLN ASTVEPLPVV TPLANKE
//
