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Database: UniProt
Entry: A5UUT1_ROSS1
LinkDB: A5UUT1_ROSS1
Original site: A5UUT1_ROSS1 
ID   A5UUT1_ROSS1            Unreviewed;       603 AA.
AC   A5UUT1;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Oligoendopeptidase, pepF/M3 family {ECO:0000313|EMBL:ABQ90384.1};
GN   OrderedLocusNames=RoseRS_1998 {ECO:0000313|EMBL:ABQ90384.1};
OS   Roseiflexus sp. (strain RS-1).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ90384.1, 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; CP000686; ABQ90384.1; -; Genomic_DNA.
DR   RefSeq; WP_011956730.1; NC_009523.1.
DR   AlphaFoldDB; A5UUT1; -.
DR   STRING; 357808.RoseRS_1998; -.
DR   KEGG; rrs:RoseRS_1998; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_3_1_0; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000006554; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09607; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR   Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR   InterPro; IPR034006; M3B_PepF_2.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR011977; Pept_M3B_clade3.
DR   InterPro; IPR001333; Peptidase_M32_Taq.
DR   NCBIfam; TIGR02290; M3_fam_3; 1.
DR   PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR   PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU003435};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   TRANSMEM        523..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          344..586
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   603 AA;  68236 MW;  1F935D9B8FDCD6F4 CRC64;
     MTLSVSEPLP HWDMTVVYPA LDSPEFNHDL TATRQAFDTM TSLFDRLGIN RRDRQSTDDA
     AVAAFETVVP ALNELLEQFS TQRAYVYSFV ATDSRNDQAQ ATFSMLMREG VRLTKLLRRL
     TAWLGGLDVE TLIQRSTIAR DHAYLVRRAA EEARHLMSPA EEELAAELDL SGGIAWARMY
     QNLTSQILVP IEREGQTVEL PMSQVRNLAR DPDRAVRRSA HEAELAAWER AALPLASALN
     SIKGQVLTLS RRRRWESPLE ASLFDNGIDR ATLDAMMTTA REFFPDFRRY LRAKARLLGL
     ERLAWYDLFA PVGSGGRSWR FSDAEAFIVA QFTRYSTRMG DFAARAFRER WIDAEPRAGK
     VGGAFCMSLR RDESRILLNH DPTADSMFTL AHELGHGYHN LNLAQQTMLN RDTPMTLAET
     ASIFCETIVR NAALQDASRD ETLEILEAFL SGACQVVVDI TSRFLFETAL FEQRATRDLS
     VAELCVLMID AQKQTYGDAL DEQTLHPFMW AVKGHYYSSG FSFYNYPYMF GLLFGLGLYA
     AYQRAPDAFQ ARYDDLLAST GLASPLELAA RMEIDLRSPA FWRASLEVIR YDIDRFESLA
     VAT
//
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