ID A0A143BMA6_9BACT Unreviewed; 1195 AA.
AC A0A143BMA6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Peptidase M1 membrane alanine aminopeptidase domain-containing protein {ECO:0000259|Pfam:PF01433};
GN ORFNames=GEMMAAP_14580 {ECO:0000313|EMBL:AMW05695.1};
OS Gemmatimonas phototrophica.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1379270 {ECO:0000313|EMBL:AMW05695.1, ECO:0000313|Proteomes:UP000076404};
RN [1] {ECO:0000313|EMBL:AMW05695.1, ECO:0000313|Proteomes:UP000076404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP64 {ECO:0000313|EMBL:AMW05695.1,
RC ECO:0000313|Proteomes:UP000076404};
RX PubMed=24821787; DOI=10.1073/pnas.1400295111;
RA Zeng Y., Feng F., Medova H., Dean J., Koblizek M.;
RT "Functional type 2 photosynthetic reaction centers found in the rare
RT bacterial phylum Gemmatimonadetes.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7795-7800(2014).
RN [2] {ECO:0000313|EMBL:AMW05695.1, ECO:0000313|Proteomes:UP000076404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP64 {ECO:0000313|EMBL:AMW05695.1,
RC ECO:0000313|Proteomes:UP000076404};
RX PubMed=26636755; DOI=10.1111/1758-2229.12363;
RA Zeng Y., Baumbach J., Barbosa E.G., Azevedo V., Zhang C., Koblizek M.;
RT "Metagenomic evidence for the presence of phototrophic Gemmatimonadetes
RT bacteria in diverse environments.";
RL Environ. Microbiol. Rep. 8:139-149(2016).
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DR EMBL; CP011454; AMW05695.1; -; Genomic_DNA.
DR RefSeq; WP_026848590.1; NZ_CP011454.1.
DR AlphaFoldDB; A0A143BMA6; -.
DR STRING; 1379270.GEMMAAP_14580; -.
DR GeneID; 78445344; -.
DR KEGG; gph:GEMMAAP_14580; -.
DR eggNOG; COG0308; Bacteria.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000076404; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF12730; ABC2_membrane_4; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076404};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 523..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 866..1071
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 1195 AA; 132715 MW; 1473173B36119C70 CRC64;
MFGPLFAFEL RGHFRRPTTW LYVAIMFFLA FFALSTEAVL TGAAMGKVKK NSPYALAQMY
AIMLAIGQII TSALVGSSVL RDFEAGVHEL VFTTRISRSG YLASKYMAAL LAMLLVFAAL
PLGAIVGSAM PWVDQETLQP INLWFYLQPF LLIGVPGVFF LSALLFSVGS LTRSAFSVYV
AGILLLVGYS VADELVRTLD RDQLANLIDP FAIRSIDLVT RYWTPVEKNA RTLPVEGFIG
INRAAWSALG ALLLAVTFRF MRLEKESRVT RKSRASKADA VVRDPVNVLP RAAGSYAPPG
MVAGWWSVTR FHAQSLVRSV PFLAIATIGL INTLMNAWYA DQNGQNRSWP MSWLMAESSI
NASFLFMLIL LTFYAGELVW RERQVKLDQV LDASPVQTAS IVLGKMSAML LLLLAFATAA
MVGTMAVQLL KGYPVLDLPV YGLYVYVADF PTWMPMVALA FLVQALVPRK PIGHVIMILV
WVSTAATANL GYDYRLLNLL STPSLRWSDL NGTGPYLQAF PAIHGYWTSI GVVLAVLAYL
SWQRGTADVP FAVRMRARFT GGTRAAVAGG LAGAGAFGGL FFYNASVLNP YFTRKEREQR
QVRYEQQWRP MERLVLPKVV AVELQVDLAP TAGTARTATS YTVLNRSGVP IDTMLLNVAA
DAAALTVTLD SVTIDRPFTT IRHDSAWGVH LLRLASPLAP GDSLRVRVVQ RFARRGFPNG
QPDRSLVENG TFFNREMFPS FGYQASNELA SDELRRKYAL PLARRGKPRT DSAGLQRQSF
LADADFVTFE ATVSTDPDQI AMAPGYLQKE WTANGRRYFH YVMDTPMPNF FSVLSARWTV
TKAMWGTVPV EVYHHPTHTF NVARMLDASK ASLAFFSQEF GPYQHRQLRI LEFPRYAGFA
QSFPNTVPYS EDIGFVARVD SSDVEDTDLP YFVTAHEIAH QWFPYQRMPA DVEGSQMLSE
SLSEYAALVV TDRQHGRAFT QKFLRAELER YLRGRAGESK GERPLTRVDL QSYIWYQKGA
IAFFALRDLI GQEALHTALR AYLDEGRFTG PPYATSLDLM RHINAATPDS LKYAIEDYFE
TITLWDVKTD SLSSTKLANG SYKVVLTATA KKLRADSLGA ETEIPMNDLV DIGVFGAAKT
GTRIGEALSL RRVRVKAGTA RYEFVVPVKP ARAGIDPYNL LIDRNPGDNS RDIGN
//