ID   BAMA_ENTCC              Reviewed;         805 AA.
AC   D5CHY0;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Outer membrane protein assembly factor BamA {ECO:0000255|HAMAP-Rule:MF_01430};
DE   Flags: Precursor;
GN   Name=bamA {ECO:0000255|HAMAP-Rule:MF_01430}; OrderedLocusNames=ECL_00980;
OS   Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC
OS   13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=716541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC
RC   279-56;
RX   PubMed=20207761; DOI=10.1128/jb.00067-10;
RA   Ren Y., Ren Y., Zhou Z., Guo X., Li Y., Feng L., Wang L.;
RT   "Complete genome sequence of Enterobacter cloacae subsp. cloacae type
RT   strain ATCC 13047.";
RL   J. Bacteriol. 192:2463-2464(2010).
RN   [2]
RP   FUNCTION IN CDI, STRAIN SPECIFICITY, MUTAGENESIS OF 550-ASP--ALA-567;
RP   675-TYR--SER-693 AND 742-GLU--VAL-752, AND EXPRESSION IN E.COLI.
RC   STRAIN=ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC
RC   279-56;
RX   PubMed=23882017; DOI=10.1128/mbio.00480-13;
RA   Ruhe Z.C., Wallace A.B., Low D.A., Hayes C.S.;
RT   "Receptor polymorphism restricts contact-dependent growth inhibition to
RT   members of the same species.";
RL   MBio 4:E00480-E00480(2013).
CC   -!- FUNCTION: Part of the outer membrane protein assembly complex, which is
CC       involved in assembly and insertion of beta-barrel proteins into the
CC       outer membrane. Constitutes, with BamD, the core component of the
CC       assembly machinery. {ECO:0000255|HAMAP-Rule:MF_01430}.
CC   -!- FUNCTION: Does not normally serve as a receptor for CdiA-EC93, the
CC       contact-dependent growth inhibition (CDI) effector of E.coli strain
CC       EC93. However if extracellular loops 6 and 7 are mutated to match the
CC       sequence of E.coli then the protein is able to act as a CdiA-EC93
CC       receptor, conferring CDI on E.coli strains expressing the mutated BamA.
CC       The same mutations also support the delivery of CdiA-CT from strain 536
CC       / UPEC. {ECO:0000269|PubMed:23882017}.
CC   -!- SUBUNIT: Part of the Bam complex, which is composed of the outer
CC       membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE.
CC       {ECO:0000255|HAMAP-Rule:MF_01430}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01430}.
CC   -!- SIMILARITY: Belongs to the BamA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01430}.
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DR   EMBL; CP001918; ADF60543.1; -; Genomic_DNA.
DR   RefSeq; WP_013095659.1; NC_014121.1.
DR   RefSeq; YP_003611492.1; NC_014121.1.
DR   AlphaFoldDB; D5CHY0; -.
DR   SMR; D5CHY0; -.
DR   STRING; 716541.ECL_00980; -.
DR   EnsemblBacteria; ADF60543; ADF60543; ECL_00980.
DR   GeneID; 60928945; -.
DR   KEGG; enc:ECL_00980; -.
DR   PATRIC; fig|716541.4.peg.1238; -.
DR   eggNOG; COG4775; Bacteria.
DR   HOGENOM; CLU_007664_1_0_6; -.
DR   OMA; IFMPAFG; -.
DR   Proteomes; UP000002363; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0051205; P:protein insertion into membrane; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01430; OM_assembly_BamA; 1.
DR   InterPro; IPR000184; Bac_surfAg_D15.
DR   InterPro; IPR010827; BamA/TamA_POTRA.
DR   InterPro; IPR039910; D15-like.
DR   InterPro; IPR023707; OM_assembly_BamA.
DR   InterPro; IPR034746; POTRA.
DR   PANTHER; PTHR12815; PTHR12815; 1.
DR   PANTHER; PTHR12815:SF23; PTHR12815:SF23; 1.
DR   Pfam; PF01103; Omp85; 1.
DR   Pfam; PF07244; POTRA; 4.
DR   PIRSF; PIRSF006076; OM_assembly_OMP85; 1.
DR   TIGRFAMs; TIGR03303; OM_YaeT; 1.
DR   PROSITE; PS51779; POTRA; 5.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Membrane; Repeat; Signal; Transmembrane;
KW   Transmembrane beta strand.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01430"
FT   CHAIN           21..805
FT                   /note="Outer membrane protein assembly factor BamA"
FT                   /id="PRO_0000432092"
FT   TOPO_DOM        21..424
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        425..433
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        434..435
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        436..446
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        447..454
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        455..462
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        463..465
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        466..475
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        476..483
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        484..495
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        496..504
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        505..506
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        507..522
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        523..535
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        536..563
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        564..577
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        578..590
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        591..600
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        601..608
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        609..619
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        620..628
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        629..639
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        640..700
FT                   /note="Extracellular; loop 6"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        701..710
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        711..724
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        725..737
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        738..762
FT                   /note="Extracellular; loop 7"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        763..772
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        773
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        774..784
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   TOPO_DOM        785..798
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        799..803
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P0A940"
FT   DOMAIN          24..91
FT                   /note="POTRA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT   DOMAIN          92..172
FT                   /note="POTRA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT   DOMAIN          175..263
FT                   /note="POTRA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT   DOMAIN          266..344
FT                   /note="POTRA 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT   DOMAIN          347..421
FT                   /note="POTRA 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT   MUTAGEN         550..567
FT                   /note="DSIGQSASTSSDNNGFAA->YSMGEHPSTSDQDNSFKT: Loop 4 to
FT                   E.coli sequence; resistant to CdiA-EC93."
FT                   /evidence="ECO:0000269|PubMed:23882017"
FT   MUTAGEN         675..693
FT                   /note="YGGNDEDNCASRDPKQVCS->FPHQASNYDPDYDYECATQDGAKDLCK:
FT                   Loop 6 to E.coli sequence; resistant to CdiA-EC93.
FT                   Susceptible to CdiA-EC93, forms aggregates with CdiA-EC93
FT                   cells; when associated with 742-D--Y-752."
FT                   /evidence="ECO:0000269|PubMed:23882017"
FT   MUTAGEN         742..752
FT                   /note="ENTAQMRAAGV->DSSQYSGY: Loop 7 to E.coli sequence;
FT                   resistant to CdiA-EC93. Susceptible to CdiA-EC93, forms
FT                   aggregates with CdiA-EC93 cells; when associated with 675-
FT                   F--K-693."
FT                   /evidence="ECO:0000269|PubMed:23882017"
SQ   SEQUENCE   805 AA;  89360 MW;  31CCB918B83E63F3 CRC64;
     MAMKKLLIAS LLFSSATVYG ADGFVVKDIH FEGLQRVAVG AALLSMPVRP GDTVNDDDIS
     NTIRALFATG NFEDVRVLRD GDTLLVQVKE RPTIASITFS GNKSVKDDML KQNLEASGVR
     VGESLDRTTL SDIEKGLEDF YYSVGKYSAS VKAVVTPLPR NRVDLKLVFQ EGVSAKIQQI
     NIVGNHAFTT DELISTFQLR DEVPWWNVVG DRKYQKQKLA GDLETLRSYY LDRGYARFNI
     DSTQVSLTPD KKGIYITINI TEGDQYKLSG VEVSGNLAGH SAEIESLTKI QPGDLYSGSK
     VTKMEDGIKK LLGRYGYAYP RVQTQPEIND ADKTVKLHVN VDAGNRFYVR KIRFEGNDTS
     KDSVLRREMR QMEGAWLGSD LVDQGKERLN RLGYFETVDT DTQRVPGSPD QVDVVYKVKE
     RNTGSFNFGV GYGTESGVSF QVGVQQDNWL GTGYSVGING TKNDYQTYSE FSVTNPYFTV
     DGVSLGGRIF YNDFKADDAD LSSYTNKSYG VDGTLGFPVN EYNTLRAGLG YVHNDLSNMQ
     PQVAMWRYLD SIGQSASTSS DNNGFAADDF TFNYGWTYNR LDRGYFPTEG SRVNLNGKVT
     IPGSDNEFYK LTLDTASYFP IDDDHKWVVL GRTRWGYGDG LGGKEMPFYE NFYAGGSSTV
     RGFQSNNIGP KAVYYGGNDE DNCASRDPKQ VCSSDDAVGG NAMAVASLEF ITPTPFISDK
     YANSVRTSFF WDAGTVWDTN WENTAQMRAA GVPDYSDPGN IRMSAGIALQ WMSPLGPLVF
     SYAQPFKKYD GDKSEQFQFN IGKTW