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
//